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1epf
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(New page: 200px<br /><applet load="1epf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1epf, resolution 1.85Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 12:04, 20 November 2007
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CRYSTAL STRUCTURE OF THE TWO N-TERMINAL IMMUNOGLOBULIN DOMAINS OF THE NEURAL CELL ADHESION MOLECULE (NCAM)
Overview
The neural cell adhesion molecule NCAM, a member of the immunoglobulin, superfamily, mediates cell-cell recognition and adhesion via a homophilic, interaction. NCAM plays a key role during development and regeneration of, the nervous system and is involved in synaptic plasticity associated with, memory and learning. The 1.85 A crystal structure of the two N-terminal, extracellular domains of NCAM reported here provides a structural basis, for the homophilic interaction. The molecular packing of the two-domain, structure reveals a cross shaped antiparallel dimer, and provides, fundamental insight into trans-cellular recognition mediated by NCAM.
About this Structure
1EPF is a Single protein structure of sequence from Rattus norvegicus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis of cell-cell adhesion by NCAM., Kasper C, Rasmussen H, Kastrup JS, Ikemizu S, Jones EY, Berezin V, Bock E, Larsen IK, Nat Struct Biol. 2000 May;7(5):389-93. PMID:10802736
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