1npe
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(New page: 200px<br /><applet load="1npe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npe, resolution 2.3Å" /> '''Crystal structure of ...)
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Revision as of 20:20, 20 November 2007
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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 with CD as ligand. 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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