1qz1
From Proteopedia
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Crystal Structure of the Ig 1-2-3 fragment of NCAM
Overview
The neural cell adhesion molecule, NCAM, mediates Ca(2+)-independent, cell-cell and cell-substratum adhesion via homophilic (NCAM-NCAM) and, heterophilic (NCAM-non-NCAM molecules) binding. NCAM plays a key role in, neural development, regeneration, and synaptic plasticity, including, learning and memory consolidation. The crystal structure of a fragment, comprising the three N-terminal Ig modules of rat NCAM has been determined, to 2.0 A resolution. Based on crystallographic data and biological, experiments we present a novel model for NCAM homophilic binding. The Ig1, and Ig2 modules mediate dimerization of NCAM molecules situated on the, same cell surface (cis interactions), whereas the Ig3 module mediates, interactions between NCAM molecules expressed on the surface of opposing, cells (trans interactions) through simultaneous binding to the Ig1 and Ig2, modules. This arrangement results in two perpendicular zippers forming a, double zipper-like NCAM adhesion complex.
About this Structure
1QZ1 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion., Soroka V, Kolkova K, Kastrup JS, Diederichs K, Breed J, Kiselyov VV, Poulsen FM, Larsen IK, Welte W, Berezin V, Bock E, Kasper C, Structure. 2003 Oct;11(10):1291-301. PMID:14527396
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