1EPF
CRYSTAL STRUCTURE OF THE TWO N-TERMINAL IMMUNOGLOBULIN DOMAINS OF THE NEURAL CELL ADHESION MOLECULE (NCAM)
1EPF の概要
| エントリーDOI | 10.2210/pdb1epf/pdb |
| 分子名称 | PROTEIN (NEURAL CELL ADHESION MOLECULE), CALCIUM ION (3 entities in total) |
| 機能のキーワード | ncam, immunoglobulin fold, glycoprotein, cell adhesion |
| 由来する生物種 | Rattus norvegicus (Norway rat) |
| 細胞内の位置 | Cell membrane; Single-pass type I membrane protein: P13596 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 85669.38 |
| 構造登録者 | Kasper, C.,Rasmussen, H.,Kastrup, J.S.,Ikemizu, S.,Jones, E.Y.,Berezin, V.,Bock, E.,Larsen, I.K. (登録日: 2000-03-29, 公開日: 2000-10-09, 最終更新日: 2024-11-20) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.85 Å) |
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