Gerstein M, Lesk A M, Chothia C
Department of Haematology, Cambridge University, U.K.
Biochemistry. 1994 Jun 7;33(22):6739-49. doi: 10.1021/bi00188a001.
We survey all the known instances of domain movements in proteins for which there is crystallographic evidence for the movement. We explain these domain movements in terms of the repertoire of low-energy conformation changes that are known to occur in proteins. We first describe the basic elements of this repertoire, hinge and shear motions, and then show how the elements of the repertoire can be combined to produce domain movements. We emphasize that the elements used in particular proteins are determined mainly by the structure of the interfaces between the domains.
我们调查了所有已知的蛋白质结构域运动实例，这些实例都有晶体学证据支持其运动。我们根据蛋白质中已知会发生的低能量构象变化来解释这些结构域运动。我们首先描述这种构象变化的基本元素，即铰链运动和剪切运动，然后展示这些元素如何组合产生结构域运动。我们强调，特定蛋白质中使用的元素主要由结构域之间界面的结构决定。
