Nanoscale studies of protein-membrane interactions in blood clotting

被引：21

作者：

Morrissey, J. H. ^{[1
]}

Tajkhorshid, E. ^{[2
,3
,4
]}

Rienstra, C. M. ^{[3
,5
]}

机构：

[1] Univ Illinois, Coll Med, Dept Biochem, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Pharmacol, Urbana, IL 61801 USA

[3] Univ Illinois, Ctr Biophys & Computat Biol, Urbana, IL 61801 USA

[4] Univ Illinois, Beckman Inst, Urbana, IL 61801 USA

[5] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

来源：

JOURNAL OF THROMBOSIS AND HAEMOSTASIS | 2011年 / 9卷

关键词：

Gla domains; membranes; phosphatidylserine; phospholipids; CARBOXYGLUTAMIC ACID DOMAIN; COAGULATION FACTOR; TISSUE-FACTOR; FACTOR VIIA; ACTIVE-SITE; FACTOR-X; SURFACE; ACTIVATION; BINDING; BILAYERS;

D O I：

10.1111/j.1538-7836.2011.04300.x

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Most of the steps in the blood clotting cascade require clotting proteins to bind to membrane surfaces with exposed phosphatidylserine. In spite of the importance of these protein-membrane interactions, we still lack a detailed understanding of how clotting proteins interact with membranes and how membranes contribute so profoundly to catalysis. Our laboratories are using multidisciplinary approaches to explore, at atomic-resolution, how blood clotting protein complexes assemble and function on membrane surfaces.

引用

页码：162 / 167

页数：6

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