1gl4
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(New page: 200px<br /> <applet load="1gl4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gl4, resolution 2.00Å" /> '''NIDOGEN-1 G2/PERLEC...)
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Revision as of 19:08, 29 October 2007
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NIDOGEN-1 G2/PERLECAN IG3 COMPLEX
Overview
Nidogen and perlecan are large multifunctional basement membrane (BM), proteins conserved in all metazoa. Their high-affinity interaction, which, is likely to contribute to BM assembly and function, is mediated by the, central G2 domain in nidogen and the third immunoglobulin (IG)-like domain, in perlecan, IG3. We have solved the crystal structure at 2.0 A resolution, of the mouse nidogen-1 G2-perlecan IG3 complex. Perlecan IG3 belongs to, the I-set of the IG superfamily and binds to the wall of the nidogen-1 G2, beta-barrel using beta-strands C, D and F. Nidogen-1 residues, participating in the extensive interface are highly conserved, whereas the, corresponding binding site on perlecan is more variable. We hypothesize, that a second, as yet unidentified, activity of nidogen overlaps ... [(full description)]
About this Structure
1GL4 is a [Protein complex] structure of sequences from [Mus musculus] with ZN and EPE as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structural basis for the high-affinity interaction of nidogen-1 with immunoglobulin-like domain 3 of perlecan., Kvansakul M, Hopf M, Ries A, Timpl R, Hohenester E, EMBO J. 2001 Oct 1;20(19):5342-6. PMID:11574465
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