STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROM RESOLUTION

被引：280

作者：

XIE, X

HARRISON, DH

SCHLICHTLING, I

SWEET, RM

KALABOKIS, VN

SZENTGYORGYI, AG

COHEN, C

机构：

[1] BRANDEIS UNIV,ROSENSTIEL BASIC MED SCI RES CTR,WALTHAM,MA 02254

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

[3] BROOKHAVEN NATL LAB,DEPT BIOL,UPTON,NY 11973

[4] BRANDEIS UNIV,DEPT BIOL,WALTHAM,MA 02254

来源：

NATURE | 1994年 / 368卷 / 6469期

关键词：

D O I：

10.1038/368306a0

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 regulatory domain of scallop myosin is a three-chain protein complex that switches on this major in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 Angstrom resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca2+-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.

引用

页码：306 / 312

页数：7

共 37 条

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