1F5W
DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN
1F5W の概要
| エントリーDOI | 10.2210/pdb1f5w/pdb |
| 関連するPDBエントリー | 1KAC |
| 分子名称 | COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR, SULFATE ION (3 entities in total) |
| 機能のキーワード | immunoglobulin v domain fold, symmetric dimer, viral protein receptor |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Single-pass type I membrane protein. Isoform 3: Secreted. Isoform 4: Secreted. Isoform 5: Secreted: P78310 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 28386.13 |
| 構造登録者 | van Raaij, M.J.,Chouin, E.,van der Zandt, H.,Bergelson, J.M.,Cusack, S. (登録日: 2000-06-18, 公開日: 2000-11-08, 最終更新日: 2024-11-13) |
| 主引用文献 | van Raaij, M.J.,Chouin, E.,van der Zandt, H.,Bergelson, J.M.,Cusack, S. Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution. Structure Fold.Des., 8:1147-1155, 2000 Cited by PubMed Abstract: The coxsackievirus and adenovirus receptor (CAR) comprises two extracellular immunoglobulin domains, a transmembrane helix and a C-terminal intracellular domain. The amino-terminal immunoglobulin domain (D1) of CAR is necessary and sufficient for adenovirus binding, whereas the site of coxsackievirus attachment has not yet been localized. The normal cellular role of CAR is currently unknown, although CAR was recently proposed to function as a homophilic cell adhesion molecule. PubMed: 11080637DOI: 10.1016/S0969-2126(00)00528-1 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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