NDLI: Resting state of the human proton channel dimer in a lipid bilayer

Content Provider	PubMed Central
Author	Li, Qufei Shen, Rong Treger, Jeremy S. Wanderling, Sherry S. Milewski, Wieslawa Siwowska, Klaudia Bezanilla, Francisco Perozo, Eduardo
Abstract	The human proton channel hHv1 is responsible for the extrusion protons during a series of important physiological events with clinical relevance. Yet, the mechanistic details underlying voltage-dependent gating, ion selectivity, and cooperativity between homodimers remain to be determined. We carried out a structural characterization of hHv1 in a lipid bilayer using spectroscopic methods and revealed a strongly focused electric field across its putative selectivity filter. In combination with computational methods, we showed that the recently determined crystal structure of CiVSD-WT is the best structural template for dimeric hHv1, and constructed a full-length model of dimeric hHv1 with spectroscopic constraints. We proposed an explicit mechanism for hHv1 gating with functional predictions according to the one-click model recently established in CiVSD.
Related Links	http://dx.doi.org/10.1073/pnas.1515043112
Starting Page	5926
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	44
Volume Number	112
Language	English
Publisher	National Academy of Sciences
Publisher Date	2015-11-03
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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