两步配体结合与协同性。一种描述肌球蛋白亚片段1与调节型肌动蛋白协同结合的模型。
Two-step ligand binding and cooperativity. A model to describe the cooperative binding of myosin subfragment 1 to regulated actin.
作者信息
Geeves M A, Halsall D J
机构信息
Department of Biochemistry, University of Bristol, United Kingdom.
出版信息
Biophys J. 1987 Aug;52(2):215-20. doi: 10.1016/S0006-3495(87)83208-3.
Abstract
The binding of actin to myosin subfragment 1 (S1) has been shown to occur as a two-step reaction. In the first step actin is weakly bound and then the complex isomerizes to the "rigor type" acto-S1 complex (Coates, J. H., A. H. Criddle, and M. A. Geeves, 1985 Biochem. J., 232:351-356). We propose here a model in which troponin/tropomyosin (Tn/Tm) controls the actin-S1 interaction by inhibiting the isomerization step. In this model the (actin)7 Tn/Tm unit is assumed to exist in two states: open and closed. S1 can bind to either of the two states but only the open form allows the isomerization reaction to take place. We demonstrate that this model can account for the cooperative binding of S1 and S1 nucleotide complexes to actin. The model provides a way of integrating both the effects of calcium and nucleotide on actin-S1 interactions.
摘要
肌动蛋白与肌球蛋白亚片段1（S1）的结合已被证明是一个两步反应。第一步，肌动蛋白被弱结合，然后复合物异构化为“僵直型”肌动蛋白 - S1复合物（科茨，J. H.，A. H. 克里德尔，和M. A. 吉夫斯，1985年，《生物化学杂志》，232:351 - 356）。我们在此提出一个模型，其中肌钙蛋白/原肌球蛋白（Tn/Tm）通过抑制异构化步骤来控制肌动蛋白 - S1相互作用。在这个模型中，（肌动蛋白）7 Tn/Tm单元被假定存在两种状态：开放和关闭。S1可以与这两种状态中的任何一种结合，但只有开放形式允许异构化反应发生。我们证明这个模型可以解释S1和S1核苷酸复合物与肌动蛋白的协同结合。该模型提供了一种整合钙和核苷酸对肌动蛋白 - S1相互作用影响的方法。
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