1gl4

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==Overview==
==Overview==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11574465 (full description)]]
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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==
==About this Structure==
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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]]. Structure known Active Site: EPE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GL4 OCA]].
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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]. Structure known Active Site: EPE. 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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:14:41 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:03:01 2007''

Revision as of 12:57, 5 November 2007


1gl4, resolution 2.00Å

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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. Structure known Active Site: EPE. 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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