CONFORMATION AND FUNCTION OF THE N-LINKED GLYCAN IN THE ADHESION DOMAIN OF HUMAN CD2

被引：304

作者：

WYSS, DF

CHOI, JS

LI, J

KNOPPERS, MH

WILLIS, KJ

ARULANANDAM, ARN

SMOLYAR, A

REINHERZ, EL

WAGNER, G

机构：

[1] HARVARD UNIV, SCH MED, DEPT BIOL CHEM & MOLEC PHARMACOL, BOSTON, MA 02115 USA

[2] PROCEPT INC, CAMBRIDGE, MA 02139 USA

[3] DANA FARBER CANC INST, IMMUNOBIOL LAB, BOSTON, MA USA

[4] HARVARD UNIV, SCH MED, DEPT MED, BOSTON, MA 02115 USA

来源：

SCIENCE | 1995年 / 269卷 / 5228期

关键词：

D O I：

10.1126/science.7544493

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 adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-(N-acetylglucosamine)(2)-(mannose)5-8] was solved by nuclear magnetic resonance. The stem and two of three branches of the carbohydrate structure are well defined and the mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather, the carbohydrate stabilizes the protein fold by counterbalancing an unfavorable clustering of five positive charges centered about lysine-61 of CD2.

引用

页码：1273 / 1278

页数：6

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