丝氨酸受体配体结合域的三维结构模型
Three-dimensional structural model of the serine receptor ligand-binding domain.
作者信息
Jeffery C J, Koshland D E
机构信息
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
出版信息
Protein Sci. 1993 Apr;2(4):559-66. doi: 10.1002/pro.5560020407.
Abstract
Computer-based homology modeling techniques were used to construct a three-dimensional model of the Escherichia coli serine receptor ligand-binding domain based on the crystal structure of the Salmonella typhimurium aspartate receptor and the sequence homology between the two receptors. Residues that have been found in mutagenesis studies to be necessary for serine binding are located in a proposed serine-binding site. Several other mutations that affect swimming behavior require relatively small shifts in alpha-carbon positions in the model to give a minimized structure, suggesting that small changes in receptor conformation can affect the signaling state of the receptor.
摘要
基于鼠伤寒沙门氏菌天冬氨酸受体的晶体结构以及两种受体之间的序列同源性，运用基于计算机的同源建模技术构建了大肠杆菌丝氨酸受体配体结合域的三维模型。在诱变研究中发现的丝氨酸结合所必需的残基位于一个推测的丝氨酸结合位点中。其他几个影响游动行为的突变需要模型中α-碳原子位置发生相对较小的移动以给出最小化结构，这表明受体构象的微小变化会影响受体的信号传导状态。
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