1gl4
From Proteopedia
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| - | [[Image:1gl4. | + | [[Image:1gl4.jpg|left|200px]]<br /><applet load="1gl4" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gl4" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1gl4, resolution 2.00Å" /> | caption="1gl4, resolution 2.00Å" /> | ||
'''NIDOGEN-1 G2/PERLECAN IG3 COMPLEX'''<br /> | '''NIDOGEN-1 G2/PERLECAN IG3 COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GL4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 1GL4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=EPE:Zn Binding Site For Chain A Symmetry Related Subunits Co ...'>EPE</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GL4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: proteoglycan]] | [[Category: proteoglycan]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:23:16 2007'' |
Revision as of 13:13, 18 December 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 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 ZN and EPE 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
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