Abstract
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.
Originalsprog | Engelsk |
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Tidsskrift | Nature Structural and Molecular Biology |
Vol/bind | 7 |
Udgave nummer | 5 |
Sider (fra-til) | 389-393 |
Antal sider | 5 |
ISSN | 1545-9993 |
DOI | |
Status | Udgivet - 2000 |