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题名:
Examining the Conservation of Kinks in Alpha Helices
作者: Law, EC; Wilman, HR; Kelm, S; Shi, JY; Deane, CM
刊名: PLOS ONE
出版日期: 2016
卷号: 11, 期号:6, 页码:
关键词: PROTEIN-COUPLED RECEPTORS ; TRANSMEMBRANE HELICES ; STRUCTURE ALIGNMENT ; MEMBRANE-PROTEINS ; DATA-BANK ; PROLINE ; DISTORTIONS ; ACTIVATION ; ALGORITHM ; FEATURES
DOI: 10.1371/journal.pone.0157553
通讯作者: Deane, CM (reprint author), Univ Oxford, Dept Stat, Oxford OX1 3TG, England.
文章类型: 期刊文献
英文摘要: Kinks are a structural feature of alpha-helices and many are known to have functional roles. Kinks have previously tended to be defined in a binary fashion. In this paper we have deliberately moved towards defining them on a continuum, which given the unimodal distribution of kink angles is a better description. From this perspective, we examine the conservation of kinks in proteins. We find that kink angles are not generally a conserved property of homologs, pointing either to their not being functionally critical or to their function being related to conformational flexibility. In the latter case, the different structures of homologs are providing snapshots of different conformations. Sequence identity between homologous helices is informative in terms of kink conservation, but almost equally so is the sequence identity of residues in spatial proximity to the kink. In the specific case of proline, which is known to be prevalent in kinked helices, loss of a proline from a kinked helix often also results in the loss of a kink or reduction in its kink angle. We carried out a study of the seven transmembrane helices in the GPCR family and found that changes in kinks could be related both to subfamilies of GPCRs and also, in a particular subfamily, to the binding of agonists or antagonists. These results suggest conformational change upon receptor activation within the GPCR family. We also found correlation between kink angles in different helices, and the possibility of concerted motion could be investigated further by applying our method to molecular dynamics simulations. These observations reinforce the belief that helix kinks are key, functional, flexible points in structures.
收录类别: SCI
语种: 英语
WOS记录号: WOS:000378030000034
ISSN号: 1932-6203
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.sinap.ac.cn/handle/331007/25720
Appears in Collections:中科院上海应用物理研究所2011-2017年_期刊论文

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Recommended Citation:
Law, EC,Wilman, HR,Kelm, S,et al. Examining the Conservation of Kinks in Alpha Helices[J]. PLOS ONE,2016-01-01,11(6):—.
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