CRYSTAL-STRUCTURE OF AN HIV-BINDING RECOMBINANT FRAGMENT OF HUMAN CD4

被引：545

作者：

RYU, SE

KWONG, PD

TRUNEH, A

PORTER, TG

ARTHOS, J

ROSENBERG, M

DAI, XP

XUONG, NH

AXEL, R

SWEET, RW

HENDRICKSON, WA

机构：

[1] COLUMBIA UNIV, HOWARD HUGHES MED INST, NEW YORK, NY 10032 USA

[2] SMITHKLINE BEECHAM PHARMACEUT, KING OF PRUSSIA, PA 19406 USA

[3] UNIV CALIF SAN DIEGO, DEPT PHYS, LA JOLLA, CA 92093 USA

[4] UNIV CALIF SAN DIEGO, DEPT CHEM, LA JOLLA, CA 92093 USA

[5] UNIV CALIF SAN DIEGO, DEPT BIOL, LA JOLLA, CA 92093 USA

来源：

NATURE | 1990年 / 348卷 / 6300期

关键词：

D O I：

10.1038/348419a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

CD4 glycoprotein on the surface of T cells helps in the immune response and is the receptor for HIV infection. The structure of a soluble fragment of CD4 determined at 2.3 Å resolution reveals that the molecule has two intimately associated immunoglobulin-like domains. Residues implicated in HIV recognition by analysis of mutants and antibody binding are salient features in domain Dl. Domain D2 is distinguished by a variation on the β-strand topologies of antibody domains and by an intra-sheet disulphide bridge. © 1990 Nature Publishing Group.

引用

页码：419 / 426

页数：8

共 59 条

[1] IDENTIFICATION OF THE RESIDUES IN HUMAN CD4 CRITICAL FOR THE BINDING OF HIV [J].