SOLUTION STRUCTURE OF CALCIUM-FREE CALMODULIN

被引:625
作者
KUBONIWA, H
TJANDRA, N
GRZESIEK, S
REN, H
KLEE, CB
BAX, A
机构
[1] NIDDKD,PHYS CHEM LAB,BETHESDA,MD 20892
[2] NCI,BIOCHEM LAB,BETHESDA,MD 20892
来源
NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 09期
关键词
D O I
10.1038/nsb0995-768
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
The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond I-couplings. In analogy with the Ca2+-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca2+, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel beta-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca2+-free N-terminal domain of troponin C.
引用
收藏
页码:768 / 776
页数:9
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