1G8Q

CRYSTAL STRUCTURE OF HUMAN CD81 EXTRACELLULAR DOMAIN, A RECEPTOR FOR HEPATITIS C VIRUS

1G8Q の概要

• エントリーDOI: 10.2210/pdb1g8q/pdb
• 分子名称: CD81 ANTIGEN, EXTRACELLULAR DOMAIN (2 entities in total)
• 機能のキーワード: alpha helical, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Basolateral cell membrane ; Multi-pass membrane protein : P60033
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19834.15

構造登録者

Kitadokoro, K.,Bolognesi, M.,Bordo, D.,Grandi, G.,Galli, G.,Petracca, R.,Falugi, F. (登録日: 2000-11-20, 公開日: 2001-02-21, 最終更新日: 2024-11-06)

主引用文献

Kitadokoro, K.,Bordo, D.,Galli, G.,Petracca, R.,Falugi, F.,Abrignani, S.,Grandi, G.,Bolognesi, M.
CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs.
EMBO J., 20:12-18, 2001

PubMed Abstract: Human CD81, a known receptor for hepatitis C virus envelope E2 glycoprotein, is a transmembrane protein belonging to the tetraspanin family. The crystal structure of human CD81 large extracellular domain is reported here at 1.6 A resolution. Each subunit within the homodimeric protein displays a mushroom-like structure, composed of five alpha-helices arranged in 'stalk' and 'head' subdomains. Residues known to be involved in virus binding can be mapped onto the head subdomain, providing a basis for the design of antiviral drugs and vaccines. Sequence analysis of 160 tetraspanins indicates that key structural features and the new protein fold observed in the CD81 large extracellular domain are conserved within the family. On these bases, it is proposed that tetraspanins may assemble at the cell surface into homo- and/or hetero-dimers through a conserved hydrophobic interface located in the stalk subdomain, while interacting with other liganding proteins, including hepatitis C virus E2, through the head subdomain. The topology of such interactions provides a rationale for the assembly of the so-called tetraspan-web.

PubMed: 11226150
DOI: 10.1093/emboj/20.1.12

実験手法

X-RAY DIFFRACTION (1.6 Å)