Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.

Tavares GA; Panepucci EH; Brunger AT

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Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.

机译：PSD-95的SH3和鸟苷酸激酶结构域之间的分子内相互作用的结构表征。

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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.

机译：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位置，并组织下游信号传导和细胞骨架分子。我们已经确定载脂蛋白和GMP结合形式的晶体结构分别为包含PSD-95的SH3，HOOK和鸟苷酸激酶（GK）域的片段的分辨率分别为2.3和2.0A。我们观察到SH3和GK域之间的分子内相互作用，涉及形成一个β片，包括GK域的N和C端残基。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蛋白之间的共同特征。

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《Molecular cell》 |2001年第6期|共13页
作者
Tavares GA; Panepucci EH; Brunger AT;
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正文语种 eng
中图分类分子生物学;细胞生物学;
关键词
Catalytic Domain; Nerve Tissue Proteins; Nucleoside-Phosphate Kinase; src Homology Domains; 催化域; 神经组织蛋白质类; 核苷一磷酸激酶; src同源域;

机译：Catalytic Domain;Nerve Tissue Proteins;Nucleoside-Phosphate Kinase;src Homology Domains;催化域;神经组织蛋白质类;核苷一磷酸激酶;src同源域;

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1. Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95. [J] . Tavares GA, Panepucci EH, Brunger AT Molecular cell . 2001,第6期

机译：PSD-95的SH3和鸟苷酸激酶结构域之间的分子内相互作用的结构表征。
2. A CaVβ SH3/Guanylate Kinase Domain Interaction Regulates Multiple Properties of Voltage-gated Ca2+ Channels [J] . Shoji X. Takahashi, Jayalakshmi Miriyala, Lai Hock Tay, The Journal of general physiology . 2005,第4期

机译：CaVβSH3 / Guanylate激酶域相互作用调节电压门控Ca2 +通道的多个属性。
3. An intramolecular interaction between Src homology 3 domain and guanylate kinase-like domain required for channel clustering by postsynaptic density-95/SAP90. [J] . Shin H, Hsueh YP, Yang FC, The Journal of Neuroscience: The Official Journal of the Society for Neuroscience . 2000,第10期

机译：Src同源性3域和鸟苷酸激酶样结构域之间的分子内相互作用，通过突触后密度95 / SAP90进行通道聚类。
4. Carboxyl Group Footprinting MS Provides Structural Insights into Inter- and Intramolecular Interactions of the Oncogenic HER2-HER3 Receptor Tyrosine Kinase Heterodimer [C] . Timothy S. Collier, John D. Monsey, Ron Bose American Society for Mass Spectrometry Conference on Mass Spectrometry and Allied Topics . 2012

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机译：质谱法以阐明蛋白质 - 蛋白质相互作用，牙买蛋白域的生化和结构表征，以及带3作为红细胞代谢和储存质量的主调节器的作用
6. Intramolecular Interactions Between the Src Homology 3 Guanylate Kinase Domains of Discs Large Regulate Its Function in Asymmetric Cell Division [O] . Rhonda A. Newman, Kenneth E. Prehoda 2009

机译：Src同源3鸟苷酸激酶之间的分子内相互作用。圆盘的区域大幅度调节其在非对称细胞中的功能师
7. Identification of an Intramolecular Interaction between the SH3 and Guanylate Kinase Domains of PSD-95 [O] . Aaron W. McGee, David S. Bredt 1999

机译：鉴定PSD-95的SH3与胍基酸激酶结构域之间的分子内相互作用

Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95.

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