1EAJ

DIMERIC STRUCTURE OF THE COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR D1 DOMAIN AT 1.35 ANGSTROM RESOLUTION

1EAJ の概要

• エントリーDOI: 10.2210/pdb1eaj/pdb
• 関連するPDBエントリー: 1F5W 1KAC
• 分子名称: COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR, SULFATE ION (3 entities in total)
• 機能のキーワード: virus/viral protein receptor, immunoglobulin v domain fold, symmetric dimer, virus-viral protein receptor complex
• 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 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: 28290.07

構造登録者

van Raaij, M.J.,Cusack, S. (登録日: 2001-07-12, 公開日: 2001-07-13, 最終更新日: 2024-10-09)

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, 8:1147-1155, 2000

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: 11080637
DOI: 10.1016/S0969-2126(00)00528-1

実験手法

X-RAY DIFFRACTION (1.35 Å)