TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential

TrkH is a bacterial ion channel that is regulated by nucleotides and its associated protein TrkA. Here the authors present ADP and ATP bound TrkH-TrkA structures, which reveal the mechanism for the transmission of nucleotide-induced conformational changes in TrkA to the opening of the TrkH channel a...

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Autores principales:	Hanzhi Zhang, Yaping Pan, Liya Hu, M. Ashley Hudson, Katrina S. Hofstetter, Zhichun Xu, Mingqiang Rong, Zhao Wang, B. V. Venkataram Prasad, Steve W. Lockless, Wah Chiu, Ming Zhou
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8f5a444b3e2548a29ca6d697a5a934a9
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spelling	oai:doaj.org-article:8f5a444b3e2548a29ca6d697a5a934a92021-12-02T15:39:16ZTrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential10.1038/s41467-019-14240-92041-1723https://doaj.org/article/8f5a444b3e2548a29ca6d697a5a934a92020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-14240-9https://doaj.org/toc/2041-1723TrkH is a bacterial ion channel that is regulated by nucleotides and its associated protein TrkA. Here the authors present ADP and ATP bound TrkH-TrkA structures, which reveal the mechanism for the transmission of nucleotide-induced conformational changes in TrkA to the opening of the TrkH channel and further support the proposed gating mechanism with functional studies.Hanzhi ZhangYaping PanLiya HuM. Ashley HudsonKatrina S. HofstetterZhichun XuMingqiang RongZhao WangB. V. Venkataram PrasadSteve W. LocklessWah ChiuMing ZhouNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hanzhi Zhang Yaping Pan Liya Hu M. Ashley Hudson Katrina S. Hofstetter Zhichun Xu Mingqiang Rong Zhao Wang B. V. Venkataram Prasad Steve W. Lockless Wah Chiu Ming Zhou TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential
description	TrkH is a bacterial ion channel that is regulated by nucleotides and its associated protein TrkA. Here the authors present ADP and ATP bound TrkH-TrkA structures, which reveal the mechanism for the transmission of nucleotide-induced conformational changes in TrkA to the opening of the TrkH channel and further support the proposed gating mechanism with functional studies.
format	article
author	Hanzhi Zhang Yaping Pan Liya Hu M. Ashley Hudson Katrina S. Hofstetter Zhichun Xu Mingqiang Rong Zhao Wang B. V. Venkataram Prasad Steve W. Lockless Wah Chiu Ming Zhou
author_facet	Hanzhi Zhang Yaping Pan Liya Hu M. Ashley Hudson Katrina S. Hofstetter Zhichun Xu Mingqiang Rong Zhao Wang B. V. Venkataram Prasad Steve W. Lockless Wah Chiu Ming Zhou
author_sort	Hanzhi Zhang
title	TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential
title_short	TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential
title_full	TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential
title_fullStr	TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential
title_full_unstemmed	TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential
title_sort	trka undergoes a tetramer-to-dimer conversion to open trkh which enables changes in membrane potential
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/8f5a444b3e2548a29ca6d697a5a934a9
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TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential

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