Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the β2-β3 loop to PDZ domain-ligand interactions
Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the β2-β3 loop to PDZ domain-ligand interactions
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DOI：
10.1016/s0022-2836(02)00544-2
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发表时间：
2002-07-19
影响因子：
5.6
通讯作者：
Ekiel, I
中科院分区：
文献类型：
--
作者：
Kozlov, G;Banville, D;Ekiel, I
已使用2D和3D杂波NMR实验确定了与鸟嘌呤核苷酸交换因子RA-GEF-2的C-末端肽复合的来自人磷酸酶hPTP 1 E的第二PDZ结构域的溶液结构。与先前解决的结构相比，hPTP 1 E复合物显示出与结合肽的C末端的扩大的相互作用表面。在PDZ结构域的长结构β 2/β 3环和肽C末端的第六个氨基酸残基之间发现了新的接触。这项工作强调了β 2/β 3环对PDZ结构域进行配体选择的重要性。(C)2002爱思唯尔科技有限公司版权所有。
The solution structure of the second PDZ domain from human phosphatase hPTP1E in complex with a C-terminal peptide from the guanine nucleotide exchange factor RA-GEF-2 has been determined using 2D and 3D heteronuclear NMR experiments. Compared to previously solved structures, the hPTP1E complex shows an enlarged interaction surface with the C terminus of the bound peptide. Novel contacts were found between the long structured beta2/beta3 loop of the PDZ domain and the sixth amino acid residue from the C terminus of the peptide. This work underlines the importance of the beta2/beta3 loop for ligand selection by PDZ domains. (C) 2002 Elsevier Science Ltd. All rights reserved.