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关于F-肌动蛋白上钙调蛋白同源结构域构象的开放或封闭情况?

An open or closed case for the conformation of calponin homology domains on F-actin?

作者信息

Lehman William, Craig Roger, Kendrick-Jones John, Sutherland-Smith Andrew J

机构信息

Department of Physiology and Biophysics, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA.

出版信息

J Muscle Res Cell Motil. 2004;25(4-5):351-8. doi: 10.1007/s10974-004-0690-7.

Abstract

Calponin homology domains link many different proteins to the surface of actin filaments. However, details of the structural interactions involved and the methods used to determine them are controversial. In the case of the actin-binding protein utrophin, for example, several models have been proposed for the binding of utrophin's calponin homology domains to actin. We review and evaluate these models and their supporting data.

摘要

钙调蛋白同源结构域将许多不同的蛋白质连接到肌动蛋白丝表面。然而,所涉及的结构相互作用细节以及用于确定这些细节的方法存在争议。例如,就肌动蛋白结合蛋白抗肌萎缩蛋白而言,已经提出了几种关于抗肌萎缩蛋白的钙调蛋白同源结构域与肌动蛋白结合的模型。我们对这些模型及其支持数据进行了综述和评估。

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