Structural basis of cell-cell adhesion by NCAM

Citation
C. Kasper et al., Structural basis of cell-cell adhesion by NCAM, NAT ST BIOL, 7(5), 2000, pp. 389-393
Citations number
43
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
10728368 → ACNP
Volume
7
Issue
5
Year of publication
2000
Pages
389 - 393
Database
ISI
SICI code
1072-8368(200005)7:5<389:SBOCAB>2.0.ZU;2-U
Abstract
The neural cell adhesion molecule NCAM, a member of the immunoglobulin supe rfamily, mediates cell-cell recognition and adhesion via a hemophilic inter action. NCAM plays a key role during development and regeneration of the ne rvous system and is involved in synaptic plasticity associated with memory and learning. The 1.85 Angstrom crystal structure of the two N-terminal ext racellular domains of NCAM reported here provides a structural basis for th e hemophilic interaction. The molecular packing of the two-domain structure reveals a cross shaped antiparallel dimer, and provides fundamental insigh t into trans-cellular recognition mediated by NCAM.