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本文引用的文献

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Hill coefficient analysis of transmembrane helix dimerization.跨膜螺旋二聚化的希尔系数分析
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Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment.近膜段激活表皮生长因子受体催化结构域的机制。
Cell. 2009 Jun 26;137(7):1293-307. doi: 10.1016/j.cell.2009.04.025.
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The juxtamembrane region of the EGF receptor functions as an activation domain.表皮生长因子受体的近膜区域作为一个激活结构域发挥作用。
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In vitro enzymatic characterization of near full length EGFR in activated and inhibited states.活化和抑制状态下近全长表皮生长因子受体（EGFR）的体外酶学特性研究
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Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers.脂质双分子层中表皮生长因子受体1跨膜结构域二聚化的能量学
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Increased expression of the integral membrane protein ErbB2 in Chinese hamster ovary cells expressing the anti-apoptotic gene Bcl-xL.在中国仓鼠卵巢细胞中，抗凋亡基因Bcl-xL表达时，整合膜蛋白ErbB2的表达增加。
Protein Expr Purif. 2009 Sep;67(1):41-7. doi: 10.1016/j.pep.2009.04.007. Epub 2009 Apr 17.
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Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains.两个类GxxxG基序促进人表皮生长因子受体（ErbB）跨膜结构域的混杂相互作用。
J Mol Biol. 2009 May 29;389(1):10-6. doi: 10.1016/j.jmb.2009.04.002. Epub 2009 Apr 8.
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The intracellular juxtamembrane domain of the epidermal growth factor (EGF) receptor is responsible for the allosteric regulation of EGF binding.表皮生长因子（EGF）受体的细胞内近膜结构域负责EGF结合的变构调节。
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Polar residues in transmembrane helices can decrease electrophoretic mobility in polyacrylamide gels without causing helix dimerization.跨膜螺旋中的极性残基可降低在聚丙烯酰胺凝胶中的电泳迁移率，而不会导致螺旋二聚化。
Biochim Biophys Acta. 2009 Jun;1788(6):1321-31. doi: 10.1016/j.bbamem.2009.02.017. Epub 2009 Mar 2.
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受体酪氨酸激酶跨膜结构域：功能、二聚体结构和二聚化能。

Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics.

机构信息

Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD, USA.

出版信息

Cell Adh Migr. 2010 Apr-Jun;4(2):249-54. doi: 10.4161/cam.4.2.10725. Epub 2010 Apr 23.

DOI:10.4161/cam.4.2.10725
PMID:20168077
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2900622/
Abstract

The transmembrane (TM) domains of receptor tyrosine kinases (RTKs) play an active role in signaling. They contribute to the stability of full-length receptor dimers and to maintaining a signaling-competent dimeric receptor conformation. In an exciting new development, two structures of RTK TM domains have been solved, a break-through achievement in the field. Here we review these structures, and we discuss recent studies of RTK TM domain dimerization energetics, possible synergies between domains, and the effects of pathogenic RTK TM mutations on structure and dimerization.

摘要

受体酪氨酸激酶 (RTK) 的跨膜 (TM) 结构域在信号转导中发挥着积极作用。它们有助于全长受体二聚体的稳定性，并维持信号传导有效的二聚体受体构象。在一个令人兴奋的新发展中，两个 RTK TM 结构域的结构已经被解决，这是该领域的一个突破成就。在这里，我们回顾这些结构，并讨论 RTK TM 结构域二聚化能学的最新研究、不同结构域之间的协同作用，以及致病 RTK TM 突变对结构和二聚化的影响。