1gl4
From Proteopedia
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|PDB= 1gl4 |SIZE=350|CAPTION= <scene name='initialview01'>1gl4</scene>, resolution 2.00Å | |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> | |SITE= <scene name='pdbsite=EPE:Zn+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>EPE</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl4 OCA], [http://www.ebi.ac.uk/pdbsum/1gl4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gl4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ries, A.]] | [[Category: Ries, A.]] | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
| - | [[Category: EPE]] | ||
| - | [[Category: ZN]] | ||
[[Category: basement membrane]] | [[Category: basement membrane]] | ||
[[Category: extracellular matrix]] | [[Category: extracellular matrix]] | ||
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[[Category: proteoglycan]] | [[Category: proteoglycan]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:46:19 2008'' |
Revision as of 17:46, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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