1EPF
CRYSTAL STRUCTURE OF THE TWO N-TERMINAL IMMUNOGLOBULIN DOMAINS OF THE NEURAL CELL ADHESION MOLECULE (NCAM)
Summary for 1EPF
| Entry DOI | 10.2210/pdb1epf/pdb |
| Descriptor | PROTEIN (NEURAL CELL ADHESION MOLECULE), CALCIUM ION (3 entities in total) |
| Functional Keywords | ncam, immunoglobulin fold, glycoprotein, cell adhesion |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P13596 |
| Total number of polymer chains | 4 |
| Total formula weight | 85669.38 |
| Authors | Kasper, C.,Rasmussen, H.,Kastrup, J.S.,Ikemizu, S.,Jones, E.Y.,Berezin, V.,Bock, E.,Larsen, I.K. (deposition date: 2000-03-29, release date: 2000-10-09, Last modification date: 2011-07-13) |
| Primary citation | Kasper, C.,Rasmussen, H.,Kastrup, J.S.,Ikemizu, S.,Jones, E.Y.,Berezin, V.,Bock, E.,Larsen, I.K. Structural basis of cell-cell adhesion by NCAM. Nat.Struct.Biol., 7:389-393, 2000 Cited by PubMed 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. PubMed: 10802736DOI: 10.1038/75165 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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