CRYSTAL-STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF A SOLUBLE FORM OF THE CELL-ADHESION MOLECULE CD2

被引：300

作者：

JONES, EY ^{[1
]}

DAVIS, SJ ^{[1
]}

WILLIAMS, AF ^{[1
]}

HARLOS, K ^{[1
]}

STUART, DI ^{[1
]}

机构：

[1] UNIV OXFORD, SIR WILLIAM DUNN SCH PATHOL, MRC, CELLULAR IMMUNOL UNIT, OXFORD OX1 3RE, ENGLAND

来源：

NATURE | 1992年 / 360卷 / 6401期

关键词：

D O I：

10.1038/360232a0

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：

The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.

引用

页码：232 / 239

页数：8

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