Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase.
Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase.
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小角度散射研究显示，基于磷酸化酶激酶催化亚基的调节结构域，钙调蛋白与两种肽的复合物具有不同的构象。
DOI：
10.1021/bi00492a003
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发表时间：
1990
期刊：
影响因子：
2.9
通讯作者：
Seeger,PA
中科院分区：
文献类型：
--
作者：
Trewhella,J;Blumenthal,DK;Rokop,SE;Seeger,PA
生命科学和物理部门，洛斯阿拉莫斯国家实验室，洛斯阿拉莫斯，新墨西哥州 87545，以及德克萨斯大学健康中心生物化学系，泰勒，泰勒，德克萨斯州 75710 收稿日期：1990 年 3 月 30 日；修订稿于 1990 年 6 月 14 日收到摘要：小角 X 射线和中子散射已用于研究与合成肽复合的钙调蛋白的溶液结构，该合成肽对应于骨骼肌磷酸化酶激酶催化亚基调节结构域中的残基 342-366 和 301-326，分别指定为 PhK5 和 PhK13。散射数据显示，PhK5 与钙调蛋白的结合诱导钙调蛋白的剧烈收缩，类似于先前当钙调蛋白与来自兔骨骼肌肌球蛋白轻链激酶的钙调蛋白结合域肽复合时观察到的情况。相反，钙调蛋白在结合 PhK13 后仍保持延伸。在两种肽存在的情况下，钙调蛋白也保持延伸。显然，PhK13 的存在抑制钙调蛋白经历 PhK5 诱导的收缩。这些数据表明，与肌球蛋白轻链激酶的催化亚基相比，磷酸化酶激酶的催化亚基存在根本不同类型的钙调蛋白-靶酶相互作用。
Life Sciences and Physics Divisions, Los Alamos National Laboratory, Los Alamos, New Mexico 87545, and Department of Biochemistry, University of Texas Health Center at Tyler, Tyler, Texas 75710 Received March 30, 1990; Revised Manuscript Received June 14, 1990 abstract: Small-angle X-ray and neutron scattering have been used to study the solution structures of calmodulin complexed with synthetic peptides corresponding to residues 342-366 and 301-326, designated PhK5 and PhK13, respectively, in the regulatory domain of the catalytic subunit of skeletal muscle phosphorylase kinase. The scattering data show that binding of PhK5 to calmodulin induces a dramatic contraction of calmodulin, similar to that previouslyobserved when calmodulin is complexed with the calmodulin-binding domain peptide from rabbit skeletalmuscle myosin light chain kinase. In contrast, calmodulin remains extended upon binding PhK13. In the presence of both peptides, calmodulin also remains extended. Apparently, the presence of PhK13 inhibits calmodulin from undergoing the PhK5-induced contraction. These dataindicate that there is a fundamentally different type of calmodulin-target enzyme interaction in the case of the catalytic subunit of phosphorylase kinase compared with that for myosin light chain kinase.