1npe
From Proteopedia
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|PDB= 1npe |SIZE=350|CAPTION= <scene name='initialview01'>1npe</scene>, resolution 2.3Å | |PDB= 1npe |SIZE=350|CAPTION= <scene name='initialview01'>1npe</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NID or NID1 or ENT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), LAMC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= NID or NID1 or ENT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), LAMC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1npe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1npe OCA], [http://www.ebi.ac.uk/pdbsum/1npe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1npe RCSB]</span> | ||
}} | }} | ||
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[[Category: Wang, J H.]] | [[Category: Wang, J H.]] | ||
[[Category: Yang, Y T.]] | [[Category: Yang, Y T.]] | ||
| - | [[Category: CD]] | ||
[[Category: basement membrane]] | [[Category: basement membrane]] | ||
[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
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[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| - | ''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 22:33:40 2008'' |
Revision as of 19:33, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | NID or NID1 or ENT (Mus musculus), LAMC1 (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Nidogen/Laminin Complex
Overview
Basement membranes are fundamental to tissue organization and physiology in all metazoans. The interaction between laminin and nidogen is crucial to the assembly of basement membranes. The structure of the interacting domains reveals a six-bladed Tyr-Trp-Thr-Asp (YWTD) beta-propeller domain in nidogen bound to laminin epidermal-growth-factor-like (LE) modules III3-5 in laminin (LE3-5). Laminin LE module 4 binds to an amphitheatre-shaped surface on the pseudo-6-fold axis of the beta-propeller, and LE module 3 binds over its rim. A Phe residue that shutters the water-filled central aperture of the beta-propeller, the rigidity of the amphitheatre, and high shape complementarity enable the construction of an evolutionarily conserved binding surface for LE4 of unprecedentedly high affinity for its small size. Hypermorphic mutations in the Wnt co-receptor LRP5 (refs 6-9) suggest that a similar YWTD beta-propeller interface is used to bind ligands that function in developmental pathways. A related interface, but shifted off-centre from the pseudo-6-fold axis and lacking the shutter over the central aperture, is used in the low-density lipoprotein receptor for an intramolecular interaction that is regulated by pH in receptor recycling.
About this Structure
1NPE is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Complex between nidogen and laminin fragments reveals a paradigmatic beta-propeller interface., Takagi J, Yang Y, Liu JH, Wang JH, Springer TA, Nature. 2003 Aug 21;424(6951):969-74. PMID:12931195
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