TARGET SEQUENCE RECOGNITION BY THE CALMODULIN SUPERFAMILY - IMPLICATIONS FROM LIGHT-CHAIN BINDING TO THE REGULATORY DOMAIN OF SCALLOP MYOSIN
TARGET SEQUENCE RECOGNITION BY THE CALMODULIN SUPERFAMILY - IMPLICATIONS FROM LIGHT-CHAIN BINDING TO THE REGULATORY DOMAIN OF SCALLOP MYOSIN
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DOI：
10.1073/pnas.92.23.10644
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发表时间：
1995-11-07
影响因子：
11.1
通讯作者：
COHEN, C
中科院分区：
文献类型：
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作者：
HOUDUSSE, A;COHEN, C
扇贝肌球蛋白调节结构域的晶体结构揭示了钙调素超家族成员与靶肽结合的一些规律。该结构表明，在这种无脊椎动物肌球蛋白的重链的IQ基序施加限制的轻链的各个叶的定位和构象。与此相反，在由Ca 2 +-CaM结合的目标中的接触残基的分析揭示了CaM的结构如何容纳更广泛的序列与该蛋白质的功能多样性相一致。
Some of the rules for how members of the calmodulin (CaM) superfamily bind to target peptides are revealed by the crystal structure of the regulatory domain of scallop myosin. The structure shows that the IQ motif of the heavy chain in this invertebrate myosin imposes constraints on both the positioning and conformation of the individual lobes of the light chains. In contrast, analysis of the contact residues in the targets bound by Ca2+-CaM reveals how the structure of CaM accommodates a broader range of sequences consonant with this protein's functional diversity.