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Reference: Lucy R. Forrest, William F. DeGrado, G.R. Dieckmann et al., (1998). Two models of the influenza A M2 channel domain: verification by comparison. Folding and Design, 3 (6), 443-448.Citable link to this page:

 

Two models of the influenza A M2 channel domain: verification by comparison

Abstract: Background: The influenza M2 protein is a simple membrane protein, containing a single transmembrane helix. It is representative of a very large family of single-transmembrane helix proteins. The functional protein is a tetramer, with the four transmembrane helices forming a proton-permeable channel across the bilayer. Two independently derived models of the M2 channel domain are compared, in order to assess the success of applying molecular modelling approaches to simple membrane proteins.Results: The Cα RSMD between the two models is 1.7 Å. Both models are composed of a left-handed bundle of helices, with the helices tilted roughly 15° relative to the (presumed) bilayer normal. The two models have similar pore radius profiles, with a pore cavity lined by the Ser31 and Gly34 residues and a pore constriction formed by the ring of His37 residues.Conclusions:Independent studies of M2 have converged on the same structural model for the channel domain. This model is in agreement with solid state NMR data. In particular, both model and NMR data indicate that the M2 helices are tilted relative to the bilayer normal and form a left-handed bundle. Such convergence suggests that, at least for simple membrane proteins, restraints-directed modelling might yield plausible models worthy of further computational and experimental investigation.

Publication status:PublishedPeer Review status:Peer reviewedVersion:Publisher's versionNotes:Copyright © 1998 Elsevier Ltd. All rights reserved. Re-use of this article is permitted in accordance with the Terms and Conditions set out at http://www.elsevier.com/open-access/userlicense/1.0/. At the time of this article's publication, Lucy R. Forrest was affiliated with the Department of Biochemistry, University of Oxford.

Bibliographic Details

Publisher: Current Biology Ltd

Publisher Website:

Host: Folding and Designsee more from them

Publication Website: http://www.sciencedirect.com/science/journal/13590278

Issue Date: 1998-November

Copyright Date: 1998

pages:443-448Identifiers

Doi: https://doi.org/10.1016/S1359-0278(98)00061-3

Issn: 1359-0278

Urn: uuid:7572d7bf-269c-418a-ad75-3506b9c46e31 Item Description

Type: Article: post-print;

Language: en

Version: Publisher's versionKeywords: influenza virus ion channel membrane protein molecular modelling transbilayer poreSubjects: Biochemistry Tiny URL: ora:8528

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Author: Lucy R. Forrest - fundingMedical Research Council - - - William F. DeGrado - - - G.R. Dieckmann - - - Mark S.P. Sansom - institut

Source: https://ora.ox.ac.uk/objects/uuid:7572d7bf-269c-418a-ad75-3506b9c46e31



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