Site-site communication in the EF-hand Ca2+-binding protein calbindin D(9k)

被引：0

作者：

Mäler L. ^{[1
,2
]}

Blankenship J. ^{[1
]}

Rance M. ^{[3
]}

Chazin W.J. ^{[1
,4
]}

机构：

[1] Dept. of Molecular Biology (MB9), Scripps Research Institute, San Diego, CA 92037

[2] Department of Biophysics, Stockholm University, Stockholm

[3] Dept. Molec. Genet., Biochem., M., University of Cincinnati, Cincinnati

[4] Department of Biochemistry, Vanderbilt University, 606 Light Hall, Nashville

来源：

Nature Structural Biology | 2000年 / 7卷 / 3期

关键词：

D O I：

10.1038/73369

中图分类号：

学科分类号：

摘要：

The cooperative binding of Ca2+ ions is an essential functional property of the EF-hand family of Ca2+-binding proteins. To understand how these proteins function, it is essential to characterize intermediate binding states in addition to the apo- and holo-proteins. The three-dimensional solution structure and fast time scale internal motional dynamics of the backbone have been determined for the half-saturated state of the N56A mutant of calbindin D(9k) with Ca2+ bound only in the N-terminal site. The extent of conformational reorganization and a loss of flexibility in the C-terminal EF-hand upon binding of an ion in the N-terminal EF-hand provide clear evidence of the importance of site-site interactions in this family of proteins, and demonstrates the strength of long-range effects in the cooperative EF-hand Ca2+-binding domain.

引用

页码：245 / 250

页数：5

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