1g8q

From Proteopedia

Revision as of 14:55, 12 November 2007

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

Overview

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.

About this Structure

1G8Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs., Kitadokoro K, Bordo D, Galli G, Petracca R, Falugi F, Abrignani S, Grandi G, Bolognesi M, EMBO J. 2001 Jan 15;20(1-2):12-8. PMID:11226150

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