1gl4
From Proteopedia
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| - | [[Image:1gl4.jpg|left|200px]] | + | [[Image:1gl4.jpg|left|200px]] |
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| - | '''NIDOGEN-1 G2/PERLECAN IG3 COMPLEX''' | + | {{Structure |
| + | |PDB= 1gl4 |SIZE=350|CAPTION= <scene name='initialview01'>1gl4</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=EPE:Zn+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>EPE</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NIDOGEN-1 G2/PERLECAN IG3 COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GL4 is a [ | + | 1GL4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11574465 11574465] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: proteoglycan]] | [[Category: proteoglycan]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:24:36 2008'' |
Revision as of 09:24, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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