STRUCTURE OF THE ACTIN-MYOSIN COMPLEX AND ITS IMPLICATIONS FOR MUSCLE-CONTRACTION

被引：1492

作者：

RAYMENT, I

HOLDEN, HM

WHITTAKER, M

YOHN, CB

LORENZ, M

HOLMES, KC

MILLIGAN, RA

机构：

[1] UNIV WISCONSIN, INST ENZYME RES, MADISON, WI 53705 USA

[2] MAX PLANCK INST MED RES, DEPT BIOPHYS, W-6900 HEIDELBERG 1, GERMANY

[3] Scripps Res Inst, DEPT CELL BIOL, LA JOLLA, CA 92037 USA

来源：

SCIENCE | 1993年 / 261卷 / 5117期

关键词：

D O I：

10.1126/science.8316858

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：

Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.

引用

页码：58 / 65

页数：8

共 57 条

[1] MAGNESIUM ION-DEPENDENT ADENOSINE-TRIPHOSPHATASE OF MYOSIN - 2-STEP PROCESSES OF ADENOSINE-TRIPHOSPHATE ASSOCIATION AND ADENOSINE-DIPHOSPHATE DISSOCIATION [J].