Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
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DOI：
10.1038/nsb0498-317
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发表时间：
1998-04-01
期刊：
影响因子：
--
通讯作者：
Br端nger, AT
中科院分区：
文献类型：
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作者：
Daniels, DL;Cohen, AR;Br端nger, AT
含有 PDZ 结构域的蛋白质有助于细胞间连接的形成以及膜蛋白受体和离子通道的定位。 PDZ 结构域与特定靶膜蛋白的 C 端残基相互作用。根据其结合特异性和序列同源性，PDZ 结构域分为两类。 II 类 PDZ 域的第一个晶体结构，即 hCASK，已通过多波长反常色散定相解决。与邻近的非晶体学相关的 PDZ 结构域的 C 端形成复合物揭示了 hCASK 与其配体之间的相互作用。 II 类 PDZ 结构域与 I 类结构域的不同之处在于形成了第二个疏水结合袋。 PDZ 结构域的 C 端羧酸盐结合环在结构上在这两类中都是保守的，表明存在广义的羧酸盐结合基序 (h-Gly-h)，其中 h 是疏水残基。
PDZ domain containing proteins assist formation of cell-cell junctions and localization of membrane protein receptors and ion channels. PDZ domains interact with the C-terminal residues of a particular target membrane protein. Based on their binding specificities and sequence homologies, PDZ domains fall into two classes. The first crystal structure of a class II PDZ domain, that of hCASK, has been solved by multi-wavelength anomalous dispersion phasing. Complex formation with the C-terminus of a neighboring non-crystallographically related PDZ domain reveals interactions between hCASK and its ligand. Class II PDZ domains differ from class I domains by formation of a second hydrophobic binding pocket. The C-terminal carboxylate binding loop of the PDZ domain is structurally conserved in both classes suggesting a generalized carboxylate binding motif (h-Gly-h) where h is a hydrophobic residue.