STRUCTURES OF THE TROPONIN-C REGULATORY DOMAINS IN THE APO AND CALCIUM-SATURATED STATES

被引：243

作者：

GAGNE, SM ^{[1
]}

TSUDA, S ^{[1
]}

LI, MX ^{[1
]}

SMILLIE, LB ^{[1
]}

SYKES, BD ^{[1
]}

机构：

[1] UNIV ALBERTA,DEPT BIOCHEM,MRC,PROT STRUCT & FUNCT GRP,EDMONTON,AB T6G 2H7,CANADA

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 09期

关键词：

D O I：

10.1038/nsb0995-784

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：

Regulation of contraction in skeletal muscle occurs through calcium binding to the protein troponin C. The solution structures of the regulatory domain of apo and calcium-loaded troponin C have been determined by multinuclear, multidimensional nuclear magnetic resonance techniques. The structural transition in the regulatory domain of troponin C on calcium binding involves an opening of the structure through large changes in interhelical angles. This leads to the increased exposure of an extensive hydrophobic patch, an event that triggers skeletal muscle contraction.

引用

页码：784 / 789

页数：6

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