Purification, analysis, and crystal structure of integrins

被引:11
作者
Xiong, Jian-Ping [1 ]
Goodman, Simon L.
Arnaout, M. Amin
机构
[1] Massachusetts Gen Hosp, Div Nephrol, Leukocyte Biol & Inflammat Program, Struct Biol Program, Charlestown, MA 02129 USA
[2] Harvard Univ, Sch Med, Charlestown, MA USA
[3] E Merck AG, Preclin Oncol Res, D-6100 Darmstadt, Germany
来源
INTEGRINS | 2007年 / 426卷
关键词
D O I
10.1016/S0076-6879(07)26014-8
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Integrins are large modular cell-surface receptors that regulate almost every aspect of cellular function through bidirectional signals transmitted across the lipid bilayer. Regulation of integrin activity is accomplished by complex and still incompletely understood biochemical pathways that modify integrin ligand binding, clustering, trafficking, and signaling functions. The dynamic tertiary and quaternary changes required to channel some of these activities have hampered, until recently, the crystal structure determination of these heterodimeric receptors. In this chapter, we review the methods used to purify and characterize these proteins biophysically and functionally, and to derive their three-dimensional structures.
引用
收藏
页码:307 / +
页数:32
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