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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.

Original publication

DOI

10.1038/75165

Type

Journal article

Journal

Nat Struct Biol

Publication Date

05/2000

Volume

7

Pages

389 - 393

Keywords

Amino Acid Sequence, Animals, Binding Sites, Calcium, Cell Adhesion, Crystallography, X-Ray, Dimerization, Heparin, Hydrogen Bonding, Immunoglobulins, Models, Molecular, Molecular Sequence Data, Neural Cell Adhesion Molecules, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Rats, Sequence Alignment, Structure-Activity Relationship