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首页> 外文期刊>Journal of Molecular Biology >Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparinto different IG modules of perlecan
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Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparinto different IG modules of perlecan

机译：Nidogens，fibulin-2，纤连蛋白和肝素的结合位点映射到不同的Perlecan IG模块上

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摘要

Perlecan, a major basement membrane proteoglycan, has a complex modular structure designed for the binding of many cellular and extracellular ligands. Its domain IV, which consists of a tandem of immunoglobulinlike modules (IG2-IG15), is rich in such binding sites, which have been mapped to different modules obtained by recombinant production. Heparin/sulfatide binding was restricted to IG5 and shown to depend on four arginine residues that are close in space in beta strands B and E of the C-type IG fold. The nidogen-1 and nidogen-2 isoforms bind to IG3 with high affinity (K-d similar to 10 nM). This interaction depends on the globular nidogen domain G2 and is crucial for the formation of ternary complexes with laminins. Two loops of IG3 located between beta strands B/C and F/G, which are spatially close, make a major contribution to binding. Fibronectin binding was localized to IG4-5 and fibulin-2 binds to IG2 and IG13-15 with different affinities. This implicates a complex cluster of heterotypic interaction sites apparently important for the supramolecular organization of perlecan in tissues.
机译：Perlecan是主要的基底膜蛋白聚糖，具有复杂的模块化结构，旨在结合许多细胞和细胞外配体。其结构域IV由一串免疫球蛋白样模块（IG2-IG15）组成，富含这样的结合位点，这些结合位点已映射到通过重组生产获得的不同模块上。肝素/硫化物的结合仅限于IG5，并显示依赖于在C型IG折叠的β链B和E中在空间上接近的四个精氨酸残基。 Nidogen-1和Nidogen-2同工型以高亲和力（类似于10 nM的K-d）与IG3结合。这种相互作用取决于球状氮素结构域G2，对于与层粘连蛋白形成三元复合物至关重要。位于β链B / C和F / G之间的两个IG3环在空间上很近，这对结合起了主要作用。纤连蛋白结合定位于IG4-5，而纤溶蛋白2以不同亲和力结合于IG2和IG13-15。这牵涉到复杂的异型相互作用位点簇，这些位点显然对组织中Perlecan的超分子组织很重要。

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