Actin: From cell biology to atomic detail

被引:92
作者
Steinmetz, MO [1 ]
Stoffler, D [1 ]
Hoenger, A [1 ]
Bremer, A [1 ]
Aebi, U [1 ]
机构
[1] DUKE UNIV, MED CTR, DEPT CELL BIOL, DURHAM, NC 27710 USA
关键词
RAY FIBER DIFFRACTION; PHALLOIDIN-BINDING-SITE; DNASE-I COMPLEX; F-ACTIN; SLIDING MOVEMENT; ATP HYDROLYSIS; CROSS-LINKING; BETA-ACTIN; 3-DIMENSIONAL RECONSTRUCTION; FILAMENT ELONGATION;
D O I
10.1006/jsbi.1997.3873
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Over the past 2 decades our knowledge about actin filaments has evolved from a rigid ''pearls on a string'' model to that of a complex, highly dynamic protein polymer which can now be analysed at atomic detail, To achieve this, exploring actin's oligomerization, polymerization, polymorphism, and dynamic behavior has been crucial to understanding in detail how this abundant and ubiquitous protein can fulfill its various functions within living cells. In this review, a correlative view of a number of distinct aspects of actin is presented, and the functional implications of recent structural, biochemical, and mechanical data are critically evaluated, Rational analysis of these various experimental data is achieved using an integrated structural approach which combines intermediate-resolution electron microscopy-based 3-D reconstructions of entire actin filaments with atomic resolution X-ray data of monomeric and polymeric actin. (C) 1997 Academic Press.
引用
收藏
页码:295 / 320
页数:26
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