1gl4
From Proteopedia
|
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 with perlecan binding and accounts for the unusually high degree of surface conservation in the G2 domain.
About this Structure
1GL4 is a Protein complex structure of sequences from Mus musculus with and as ligands. Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 12:51:20 2008
