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Meet the faces who are Scotland THEY range from a 14 year old schoolgirl to an African beauty queen and in a stunning Christmas shoot these stunning youngsters showed they had what it takes to be future stars of the catwalk. THEY range from a 14 year old schoolgirl to an African beauty queen and in a stunning Christmas shoot these stunning youngsters showed they had what it takes to be future stars of the catwalk. THEY range from a 14 year old schoolgirl to an African beauty queen and in a stunning Christmas shoot these stunning youngsters showed they had what it takes to be future stars of the catwalk.+1 THEY range from a 14 year old schoolgirl to an African beauty queen and in a stunning Christmas shoot these stunning youngsters showed they had what it takes to be future stars of the catwalk. MEET Scotland s next top models the rising stars of 2013. From a 14 year old schoolgirl to an African beauty queen, these starlets are tipped to follow in the footsteps of Scots supermodels such as Kirsty Hume and Amanda Hendrick. In our festive shoot, these stunning youngsters prove they have what it takes to be stars of the future. They are all signed to leading model agency Colours and some have already landed big gigs with fashion giants, including Chanel and Abercrombie. Wearing antlers and T shirts with the slogan "A model is for life, not just for Christmas", our festive photoshoot is the perfect showcase. Rosalynd Ramage, Colours director, said: "These amazing young people are going to go down a storm in the industry. They are young and edgy and ready to put in the hard work needed to have a successful career." Jordan ThompsonJordan (pictured top right) has always dreamed of being a model but never imagined his first job would be with fashion giants Chanel. The 17 year old son of Sunday Mail Great Scot Joyce Young was one of just 30 male models chosen to walk VIP guests down the red carpet at Karl Lagerfeld s Chanel show at Linlithgow Palace. Jordan, whose older brother James was stabbed to death five years ago, was spotted by Colours at our Great Scots event when his mum was hailed for her work with the families of murder victims. He said: "James would find it amusing that I ve been signed as a model and got to work for Chanel. He would tease me and call me a poser but, deep down, he would be proud of me. "He d think it was cool I ve landed a job where I get paid to be surrounded by pretty girls. "Working at the Chanel show was exciting and gave me an insight into the world of fashion. It s something I want to pursue. "People ask me why I am not more excited about being picked as a model but that s just me I m laid back. "My brother being killed is the worst thing that could happen so I just take everything in my stride. That s how I cope. I can t afford to get too excited or too sad about things." Jordan, from Blackhill, Glasgow, who is studying for his Highers, was shocked when Colours director Rosalynd Ramage approached him at the awards. The St Aloysius pupil, who accompanied Joyce, 40, on stage when she received her award, thought Rosalynd was joking. Jordan s mum Joyce Young, left, won the Sunday Mail Great Scot Award He said: "My mum has been nagging me for two years about getting a job, telling me work doesn t just land in your lap.2 chain harbouring binding sites for 2, burberry fashion3, burberry fashion Rupert 2 and Erhard, fashion1,41The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The Cterminus of the laminin chain contains a tandem of five laminin Glike (LG) domains. We report the 2.0 crystal structure of the laminin 2 LG4 LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor dystroglycan, and is 41% identical to the laminin 1 E3 fragment. LG4 and LG5 are arranged in a Vshaped fashion related by a 110 rotation about an axis passing near the domain termini. An extended Nterminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind dystroglycan and heparin. The LG4 LG5 structure was used to construct a model of the laminin LG1 LG5 tandem and interpret missense mutations underlying protein S deficiency. Basement membranes are specialized sheetlike extracellular matrices that underlie epithelial and endothelial cell sheets and surround muscle cells, fat cells and peripheral nerve axons. The supramolecular structure of basement membranes derives largely from extensive protein networks formed by collagen IV and laminin ( and , 1996). The laminins constitute a family of heterotrimeric () glycoproteins with diverse and crucial functions in basement membrane assembly and function ( and , 1998). Five, three and three chains have been identified to date, which associate to form at least 12 laminin isoforms ( and , 1998; et al., 1999; Koch et al., 1999). Laminin 1 (111) and the closely related laminin 2 (211) are crossshaped molecules (Beck et al., 1990). All three chains contribute to the helical coiledcoil that forms the long arm of the cross, whereas the short arms are composed of one chain each. The Nterminal globular domains at the tips of the short arms mediate the calciumdependent polymerization of laminins 1 and 2 into a polygonal network ( and , 1993). The chains are unique in that they contain at their Ctermini a tandem of five laminin Glike (LG) domains, LG1 LG5. The Cterminal LG4 LG5 pair, which in the case of the 1 chain can be released by limited proteolysis (E3 fragment), harbours binding sites for heparin, sulfatides and the cell surface receptor dystroglycan (Ott et al., 1982; and , 1993; Gee et al., 1993; , 1993; Sung et al., 1993; et al., 1999). dystroglycan (DG), the extracellular portion of the dystroglycan transmembrane complex ( and , 1999), plays an important role in basement membrane assembly by binding and organizing soluble laminin at the cell surface, thereby facilitating the polymerization process ( and , 1998; Colognato et al., 1999; et al., 1999). Laminin 1 is present characteristically in epithelial tissues ( and , 1998), where DG additionally may bind to the LG domains of the major basement membrane proteoglycan perlecan ( et al., 1999). In muscle, the DG laminin 2 complex provides a crucial linkage of the cytoskeleton to the extracellular matrix, and mutations in the laminin 2 chain result in muscular dystrophy ( and , 1999). In nerve cells, DG supports Schwann cell adhesion to laminins 1 and 2 ( et al., 1994, 1996). The DG laminin 2 complex also serves as an attachment site for Mycobacterium leprae during Schwann cell penetration ( et al., 1998). Structure function studies of laminins have long been hampered by the difficulty of obtaining recombinant fragments of the LG1 LG5 tandem. We have recently been able to obtain individual LG domains, as well as LG tandems, in recombinant form by expression in mammalian cells ( et al., 1998; et al., 1999). This has allowed a precise mapping of binding sites on the LG4 LG5 tandem. Moncler Kids Down Jacket Multiple Logo Sky Grey In the laminin 1 chain, the binding sites for heparin, sulfatides and DG are contained within LG4, and sitedirected mutagenesis of basic residues has identified several regions as important for ligand binding ( et al., 1999). In contrast, in the related 2 chain, only the LG4 LG5 pair, but not the individual LG domains, supports highaffinity DG binding. Heparin binds to LG5 alone, albeit less strongly than to the LG4 LG5 pair ( et al., 1999). We have recently solved the crystal structure of the laminin 2 chain LG5 domain (2LG5), which revealed a 14stranded sandwich with similarity to the pentraxins ( et al., 1999). The calcium dependence of DG binding could be explained by the presence of a conserved calcium site on 2LG5, which was suggested to bind directly to the anionic sugar moieties of DG. In addition, several lysine residues in LG5 were found to be important for DG and heparin binding to the laminin 2 chain ( et al., 1999). The structure of a single LG domain from the neuronal cell recognition molecule neurexin I was also reported recently ( et al., 1999). This LG domain is similar to 2LG5, but lacks the calciumbinding site conserved in laminins, agrin and perlecan ( et al., 1999). To understand how the LG4 and LG5 domains in laminin 2 cooperate in DG binding, we have now determined the structure of the laminin 2 chain LG4 LG5 pair (2LG4 5). The apparently rigid 2LG4 5 tandem is seen to use an extensive basic surface region bounded by the conserved calciumbinding sites to bind DG. The boundaries of the construct were chosen to match the well characterized proteolytic E3 fragment of the homologous laminin 1 chain (Ott et al., 1982; et al., 1988). Thus, the LG4 module in 2LG4 5 is preceded by an Nterminal segment of 30 residues containing a single cysteine, Cys2747. The 2LG4 5 crystal structure was solved by a combination of molecular replacement (MR) and single isomorphous replacement (SIR) and refined to 2.0 resolution (Tables I and II). The first and last residue defined by the electron density are His2744 and Thr3117, respectively. The first 19 residues including the APLA sequence are disordered in the crystal. The 2LG4 5 tandem bears an Nlinked glycan attached to Asn2889 in LG4 ( et al., 1998). Moncler Men 2014 This residue is located in a mobile loop segment and, as only weak density is observed for the sugar moieties, no attempts were made to include the glycan in the model. View this table:View popupView inline Table 1. Data collection and phasing statisticsa View this table:View popupView inline Table 2. Refinement statistics The structure of 2LG4 5 The 2LG4 5 structure has approximate overall dimensions of 35 40 80. Both LG domains, LG4 and LG5, are built up from the typical 14stranded antiparallel sandwich with a disulfide bridge near the domain termini and a calciumbinding site at the opposite edge of the sandwich ( et al., 1999; et al., 1999). In the 2LG4 5 tandem, the two domains are arranged in a Vshaped fashion such that their termini are located close to the domain interface at the bottom of the V, while the calciumbinding sites are situated at the tips of the domains at 65 from one another (Figure 1). LG4 and LG5 are related by an almost pure rotation of 110 about an axis passing near the domain termini. This arrangement is forced by the close proximity of the domain termini and is unusual for tandemly repeated domains, which commonly have their termini at opposite ends of the domain (Bork et al., 1996). The portion of the Nterminal segment that is defined by the electron density extends 30 away from LG4, running alongside LG5 and forming a disulfide bridge to the helical turn in LG5 situated opposite the calcium site (Cys2747 Cys3017). This unexpected structural feature results in the pairing of all cysteines in 2LG4 5. The Nterminal segment also greatly strengthens the association between LG4 and LG5, making the 2LG4 5 tandem a rigid structure with limited potential for domain flexing. The disordered portion of the Nterminus, which is unusual in that it contains many prolines and hydrophobic residues, is likely to interact with some part of LG1 LG3 in the complete laminin LG1 LG5 tandem. Our previous 2LG5 structure ( et al., 1999) allowed the intradomain disulfide bridges in the laminin LG1 LG5 tandem to be assigned with confidence (two in LG1 and one each in the other LG domains). The present 2LG4 5 structure has revealed an unusual interdomain bridge between the LG3 LG4 linker and LG5. Thus, we can account for all 14 cysteines present in the laminin 1 and 2 chain LG1 LG5 tandems, finally clarifying a confusing issue. The interface between LG4 and LG5 Neglecting the Nterminal segment (Ser2729 Gly2758), 430 2 of accessible surface area are buried in the LG4 LG5 interface (Figure 2A). The interface is constructed entirely from the N and Cterminal portions of both LG domains. LG4 contributes strand A, the A B turn and the loop following strand N, whereas LG5 contributes the M N turn, strands Y and Z and their associated turns. The interface is formed from both hydrophobic and polar residues, but there is only one direct hydrogen bond between LG4 and LG5, involving Glu2792 and the amide nitrogen atom of Ser2936. The most prominent hydrophobic contact involves Phe2931, which packs against Gln3111, Pro3116 and Tyr2939 of LG5. In addition, Leu2764 in the LG4 A B turn contacts Pro3112 and Val3113 of LG5. It is noteworthy that almost all of the key interface residues cluster near the conserved intradomain disulfide bridges of both LG4 and LG5. At the back of the interface (in the view of Figure 2A), there is a shallow cavity lined by polar residues, among them Gln2761, Glu2792, Asp2903 and Ser3114, which contains several ordered water molecules mediating indirect contacts between LG4 and LG5. In the 2LG4 5 tandem, the first and last residues of LG5 form a small antiparallel sheet. The two strands, termed Y and Z, were not observed in the structure of the isolated LG5 domain ( et al., 1999), even though the corresponding residues (2933 2935 and 3115 3117, respectively) were present in the construct. Evidently, their conformation is dependent on the stabilizing influence of the adjacent LG4 domain, and the small Y Z sheet should thus be regarded as a feature of the LG4 LG5 domain interface2 chain harbouring binding sites for 2, burberry fashion3, burberry fashion Rupert 2 and Erhard, fashion1,41The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The Cterminus of the laminin chain contains a tandem of five laminin Glike (LG) domains. We report the 2.0 crystal structure of the laminin 2 LG4 LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor dystroglycan, and is 41% identical to the laminin 1 E3 fragment. LG4 and LG5 are arranged in a Vshaped fashion related by a 110 rotation about an axis passing near the domain termini. An extended Nterminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind Mens Moncler Jackets Cheap dystroglycan and heparin. The LG4 LG5 structure was used to construct a model of the laminin LG1 LG5 tandem and interpret missense mutations underlying protein S deficiency. Basement membranes are specialized sheetlike extracellular matrices that underlie epithelial and endothelial cell sheets and surround muscle cells, fat cells and peripheral nerve axons. The supramolecular structure of basement membranes derives largely from extensive protein networks formed by collagen IV and laminin ( and , 1996). The laminins constitute a family of heterotrimeric () glycoproteins with diverse and crucial functions in basement membrane assembly and function ( and , 1998). Five, three and three chains have been identified to date, which associate to form at least 12 laminin isoforms ( and , 1998; et al., 1999; Koch et al., 1999). Laminin 1 (111) and the closely related laminin 2 (211) are crossshaped molecules (Beck et al., 1990). All three chains contribute to the helical coiledcoil that forms the long arm of the cross, whereas the short arms are composed of one chain each. The Nterminal globular domains at the tips of the short arms mediate the calciumdependent polymerization of laminins 1 and 2 into a polygonal network ( and , 1993). The chains are unique in that they contain at their Ctermini a tandem of five laminin Glike (LG) domains, LG1 LG5. The Cterminal LG4 LG5 pair, which in the case of the 1 chain can be released by limited proteolysis (E3 fragment), harbours binding sites for heparin, sulfatides and the cell surface receptor dystroglycan (Ott et al., 1982; and , 1993; Gee et al., 1993; , 1993; Sung et al., 1993; et al., 1999). dystroglycan (DG), the extracellular portion of the dystroglycan transmembrane complex ( and , 1999), plays an important role in basement membrane assembly by binding and organizing soluble laminin at the cell surface, thereby facilitating the polymerization process ( and , 1998; Colognato et al., 1999; et al., 1999). Laminin 1 is present characteristically in epithelial tissues ( and , 1998), where DG additionally may bind to the LG domains of the major basement membrane proteoglycan perlecan ( et al., 1999). In muscle, the DG laminin 2 complex provides a crucial linkage of the cytoskeleton to the extracellular matrix, and mutations in the laminin 2 chain result in muscular dystrophy ( and , 1999). In nerve cells, DG supports Schwann cell adhesion to laminins 1 and 2 ( et al., 1994, 1996). The DG laminin 2 complex also serves as an attachment site for Mycobacterium leprae during Schwann cell penetration ( et al., 1998). Structure function studies of laminins have long been hampered by the difficulty of obtaining recombinant fragments of the LG1 LG5 tandem. We have recently been able to obtain individual LG domains, as well as LG tandems, in recombinant form by expression in mammalian cells ( et al., 1998; et al., 1999). This has allowed a precise mapping of binding sites on the LG4 LG5 tandem. In the laminin 1 chain, the binding sites for heparin, sulfatides and DG are contained within LG4, and sitedirected mutagenesis of basic residues has identified several regions as important for ligand binding ( et al., 1999). In contrast, in the related 2 chain, only the LG4 LG5 pair, but not the individual LG domains, supports highaffinity DG binding. Heparin binds to LG5 alone, albeit less strongly than to the LG4 LG5 pair ( et al., 1999). We have recently solved the crystal structure of the laminin 2 chain LG5 domain (2LG5), which revealed a 14stranded sandwich with similarity to the pentraxins ( et al., 1999). The calcium dependence of DG binding could be explained by the presence of a conserved calcium site on 2LG5, which was suggested to bind directly to the anionic sugar moieties of DG. In addition, several lysine residues in LG5 were found to be important for DG and heparin binding to the laminin 2 chain ( et al., 1999). The structure of a single LG domain from the neuronal cell recognition molecule neurexin I was also reported recently ( et al., 1999). This LG domain is similar to 2LG5, but lacks the calciumbinding site conserved in laminins, agrin and perlecan ( et al., 1999). To understand how the LG4 and LG5 domains in laminin 2 cooperate in DG binding, we have now determined the structure of the laminin 2 chain LG4 LG5 pair (2LG4 5). The apparently rigid 2LG4 5 tandem is seen to use an extensive basic surface region bounded by the conserved calciumbinding sites to bind DG. The boundaries of the construct were chosen to match the well characterized proteolytic E3 fragment of the homologous laminin 1 chain (Ott et al., 1982; et al., 1988). Thus, the LG4 module in 2LG4 5 is preceded by an Nterminal segment of 30 residues containing a single cysteine, Cys2747. The 2LG4 5 crystal structure was solved by a combination of molecular replacement (MR) and single isomorphous replacement (SIR) and refined to 2.0 resolution (Tables I and II). The first and last residue defined by the electron density are His2744 and Thr3117, respectively. The first 19 residues including the APLA sequence are disordered in the crystal. The 2LG4 5 tandem bears an Nlinked glycan attached to Asn2889 in LG4 ( et al., 1998). This residue is located in a mobile loop segment and, as only weak density is observed for the sugar moieties, no attempts were made to include the glycan in the model. View this table:View popupView inline Table 1. Data collection and phasing statisticsa View this table:View popupView inline Table 2. Refinement statistics The structure of 2LG4 5 The 2LG4 5 structure has approximate overall dimensions of 35 40 80. Both LG domains, LG4 and LG5, are built up from the typical 14stranded antiparallel sandwich with a disulfide bridge near the domain termini and a calciumbinding site at the opposite edge of the sandwich ( et al., 1999; et al., 1999). In the 2LG4 5 tandem, the two domains are arranged in a Vshaped fashion such that their termini are located close to the domain interface at the bottom of the V, while the calciumbinding sites are situated at the tips of the domains at 65 from one another (Figure 1). LG4 and LG5 are related by an almost pure rotation of 110 about an axis passing near the domain termini. This arrangement is forced by the close proximity of the domain termini and is unusual for tandemly repeated domains, which commonly have their termini at opposite ends of the domain (Bork et al., 1996). The portion of the Nterminal segment that is defined by the electron density extends 30 away from LG4, running alongside LG5 and forming a disulfide bridge to the helical turn in LG5 situated opposite the calcium site (Cys2747 Cys3017). This unexpected structural feature results in the pairing of all cysteines in 2LG4 5. The Nterminal segment also greatly strengthens the association between LG4 and LG5, making the 2LG4 5 tandem a rigid structure with limited potential for domain flexing. The disordered portion of the Nterminus, which is unusual in that it contains many prolines and hydrophobic residues, is likely to interact with some part of LG1 LG3 in the complete laminin LG1 LG5 tandem. Our previous 2LG5 structure ( et al., 1999) allowed the intradomain disulfide bridges in the laminin LG1 LG5 tandem to be assigned with confidence (two in LG1 and one each in the other LG domains). The present 2LG4 5 structure has revealed an unusual interdomain bridge between the LG3 LG4 linker and LG5. Thus, we can account for all 14 cysteines present in the laminin 1 and 2 chain LG1 LG5 tandems, finally clarifying a confusing issue. The interface between LG4 and LG5 Neglecting the Nterminal segment (Ser2729 Gly2758), 430 2 of accessible surface area are buried in the LG4 LG5 interface (Figure 2A). The interface is constructed entirely from the N and Cterminal portions of both LG domains. LG4 contributes strand A, the A B turn and the loop following strand N, whereas LG5 contributes the M N turn, strands Y and Z and their associated turns. The interface is formed from both hydrophobic and polar residues, but there is only one direct hydrogen bond between LG4 and LG5, involving Glu2792 and the amide nitrogen atom of Ser2936. The most prominent hydrophobic contact involves Phe2931, which packs against Gln3111, Pro3116 and Tyr2939 of LG5. In addition, Leu2764 in the LG4 A B turn contacts Pro3112 and Val3113 of LG5. It is noteworthy that almost all of the key interface residues cluster near the conserved intradomain disulfide bridges of both LG4 and LG5. At the back of the interface (in the view of Figure 2A), there is a shallow cavity lined by polar residues, among them Gln2761, Glu2792, Asp2903 and Ser3114, which contains several ordered water molecules mediating indirect contacts between LG4 and LG5. In the 2LG4 5 tandem, the first and last residues of LG5 form a small antiparallel sheet. The two strands, termed Y and Z, were not observed in the structure of the isolated LG5 domain ( et al., 1999), even though the corresponding residues (2933 2935 and 3115 3117, respectively) were present in the construct. Evidently, their conformation is dependent on the stabilizing influence of the adjacent LG4 domain, and the small Y Z sheet should thus be regarded as a feature of the LG4 LG5 domain interface