CALCIUM-INDUCED CONFORMATIONAL TRANSITION REVEALED BY THE SOLUTION STRUCTURE OF APO CALMODULIN
CALCIUM-INDUCED CONFORMATIONAL TRANSITION REVEALED BY THE SOLUTION STRUCTURE OF APO CALMODULIN
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DOI：
10.1038/nsb0995-758
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发表时间：
1995-09-01
期刊：
影响因子：
--
通讯作者：
IKURA, M
中科院分区：
文献类型：
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作者：
ZHANG, M;TANAKA, T;IKURA, M
用核磁共振波谱测定了无钙钙调素的溶液结构，并与以前报道的钙饱和形式的结构进行了比较。钙的去除导致四个EF-手基序的螺旋角增加了36度-44度，这导致了表面性质的重大变化，包括关闭了靶蛋白识别所必需的深疏水空腔，螺旋A和D相对于B和C，螺旋E和H相对于F和G APE，这可能是氨基和羧基末端两个相邻的EF-手部位协同结合钙的原因。
The solution structure of Ca2+-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca2+-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees, This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition, Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G ape likely responsible for the cooperative Ca2+-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.