Structural basis of cell-cell adhesion by NCAM
Research output: Contribution to journal › Journal article › Research › peer-review
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 language | English |
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Journal | Nature Structural and Molecular Biology |
Volume | 7 |
Issue number | 5 |
Pages (from-to) | 389-393 |
Number of pages | 5 |
ISSN | 1545-9993 |
DOIs | |
Publication status | Published - 2000 |
- 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
Research areas
ID: 177814