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本文引用的文献

1
Improvements in G protein-coupled receptor purification yield light stable rhodopsin crystals.G蛋白偶联受体纯化方法的改进产生了光稳定的视紫红质晶体。
J Struct Biol. 2006 Dec;156(3):497-504. doi: 10.1016/j.jsb.2006.05.003. Epub 2006 Jun 2.
2
Coupling ligand structure to specific conformational switches in the beta2-adrenoceptor.将β2肾上腺素能受体中的配体结构与特定构象转换相耦合。
Nat Chem Biol. 2006 Aug;2(8):417-22. doi: 10.1038/nchembio801. Epub 2006 Jun 25.
3
Metal ion site engineering indicates a global toggle switch model for seven-transmembrane receptor activation.金属离子位点工程揭示了七跨膜受体激活的全局切换开关模型。
J Biol Chem. 2006 Jun 23;281(25):17337-17346. doi: 10.1074/jbc.M512510200. Epub 2006 Mar 27.
4
Use of an in situ disulfide cross-linking strategy to study the dynamic properties of the cytoplasmic end of transmembrane domain VI of the M3 muscarinic acetylcholine receptor.使用原位二硫键交联策略研究M3毒蕈碱型乙酰胆碱受体跨膜结构域VI胞质端的动态特性。
Biochemistry. 2006 Jan 24;45(3):676-85. doi: 10.1021/bi051503q.
5
Molecular basis of inverse agonism in a G protein-coupled receptor.G蛋白偶联受体中反向激动作用的分子基础。
Nat Chem Biol. 2005 Jun;1(1):25-8. doi: 10.1038/nchembio705. Epub 2005 May 24.
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Calindol, a positive allosteric modulator of the human Ca(2+) receptor, activates an extracellular ligand-binding domain-deleted rhodopsin-like seven-transmembrane structure in the absence of Ca(2+).卡林多，一种人钙（2+）受体的正变构调节剂，在无钙（2+）的情况下激活了一个缺失细胞外配体结合结构域的视紫红质样七跨膜结构。
J Biol Chem. 2005 Nov 4;280(44):37013-20. doi: 10.1074/jbc.M506681200. Epub 2005 Aug 31.
7
Identification of an agonist-induced conformational change occurring adjacent to the ligand-binding pocket of the M(3) muscarinic acetylcholine receptor.鉴定在M(3)毒蕈碱型乙酰胆碱受体配体结合口袋附近发生的激动剂诱导的构象变化。
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8
Structure of rhodopsin and the metarhodopsin I photointermediate.视紫红质及视紫红质I光中间体的结构。
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Transduction of receptor signals by beta-arrestins.β-抑制蛋白介导的受体信号转导
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10
Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists.用儿茶酚对β2肾上腺素能受体结合位点进行探测，揭示了激动剂和部分激动剂在结合和激活方面的差异。
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G蛋白偶联受体的结构与激活

G protein coupled receptor structure and activation.

作者信息

Kobilka Brian K

机构信息

Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.

出版信息

Biochim Biophys Acta. 2007 Apr;1768(4):794-807. doi: 10.1016/j.bbamem.2006.10.021. Epub 2006 Nov 15.

DOI:10.1016/j.bbamem.2006.10.021
PMID:17188232
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1876727/
Abstract

G protein coupled receptors (GPCRs) are remarkably versatile signaling molecules. The members of this large family of membrane proteins are activated by a spectrum of structurally diverse ligands, and have been shown to modulate the activity of different signaling pathways in a ligand specific manner. In this manuscript I will review what is known about the structure and mechanism of activation of GPCRs focusing primarily on two model systems, rhodopsin and the beta(2) adrenoceptor.

摘要

G蛋白偶联受体（GPCRs）是极为多功能的信号分子。这个大家族的膜蛋白成员可被一系列结构多样的配体激活，并已证明能以配体特异性的方式调节不同信号通路的活性。在本论文中，我将主要围绕视紫红质和β2肾上腺素能受体这两个模型系统，综述关于GPCRs激活的结构和机制的已知信息。