Three-dimensional structural model of the serine receptor ligand-binding domain.
Three-dimensional structural model of the serine receptor ligand-binding domain.
复制标题
丝氨酸受体配体结合域的三维结构模型。
DOI：
10.1002/pro.5560020407
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
KoshlandJr,DE
中科院分区：
文献类型：
--
作者：
Jeffery,CJ;KoshlandJr,DE
基于天冬氨酸鼠伤寒沙门氏菌受体的晶体结构和两种受体之间的序列同源性，使用基于计算机的同源性建模技术构建大肠杆菌受体配体结合结构域的三维模型。在诱变研究中发现丝氨酸结合所必需的残基位于拟定的丝氨酸结合位点。其他几个影响游泳行为的突变需要模型中α-碳位置相对较小的位移，以获得最小化的结构，这表明受体构象的微小变化可以影响受体的信号状态。
Computer‐based homology modeling techniques were used to construct a three‐dimensional model of theEscherichia coliserine receptor ligand‐binding domain based on the crystal structure of theSalmonella typhimuriumaspartate 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 inα‐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.