Tavares G A, Panepucci E H, Brunger A T
The Howard Hughes Medical Institute and Department of Molecular and Cellular Physiology, Stanford University, 1201 Welch Road P210 MSLS, Stanford, CA 94305, USA.
Mol Cell. 2001 Dec;8(6):1313-25. doi: 10.1016/s1097-2765(01)00416-6.
PSD-95/SAP90 is a member of the MAGUK superfamily. In excitatory synapses, PSD-95 clusters receptors and ion channels at specific sites in the postsynaptic membrane and organizes downstream signaling and cytoskeletal molecules. We have determined the crystal structures of the apo and GMP-bound forms to 2.3 and 2.0 A resolutions, respectively, of a fragment containing the SH3, HOOK, and guanylate kinase (GK) domains of PSD-95. We observe an intramolecular interaction between the SH3 and GK domains involving the formation of a beta sheet including residues N- and C-terminal to the GK domain. Based on amino acid conservation and mutational data available in the literature, we propose that this intramolecular interaction is a common feature among MAGUK proteins.
PSD - 95/SAP90是MAGUK超家族的成员。在兴奋性突触中，PSD - 95将受体和离子通道聚集在突触后膜的特定部位，并组织下游信号传导和细胞骨架分子。我们分别以2.3埃和2.0埃的分辨率确定了包含PSD - 95的SH3、HOOK和鸟苷酸激酶（GK）结构域的片段的无配体形式和GMP结合形式的晶体结构。我们观察到SH3和GK结构域之间存在分子内相互作用，涉及形成一个β折叠，该β折叠包括GK结构域N端和C端的残基。基于文献中可用的氨基酸保守性和突变数据，我们提出这种分子内相互作用是MAGUK蛋白的一个共同特征。
