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Viral ion channels: molecular modeling and simulation
Author(s) -
Sansom Mark S.P.,
Forrest Lucy R.,
Bull Richard
Publication year - 1998
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(199812)20:12<992::aid-bies5>3.0.co;2-7
Subject(s) - transmembrane domain , transmembrane protein , ion channel , biophysics , helix (gastropod) , membrane protein , solid state nuclear magnetic resonance , chemistry , integral membrane protein , membrane , computational biology , biology , physics , biochemistry , nuclear magnetic resonance , ecology , receptor , snail
In a number of membrane‐bound viruses, ion channels are formed by integral membrane proteins. These channel proteins include M2 from influenza A, NB from influenza B, and, possibly, Vpu from HIV‐1. M2 is important in facilitating uncoating of the influenza A viral genome and is the target of amantadine, an anti‐influenza drug. The biological roles of NB and Vpu are less certain. In all cases, the protein contains a single transmembrane α‐helix close to its N‐terminus. Channels can be formed by homo‐oligomerization of these proteins, yielding bundles of transmembrane helices that span the membrane and surround a central ion‐permeable pore. Molecular modeling may be used to integrate and interpret available experimental data concerning the structure of such transmembrane pores. This has proved successful for the M2 channel domain, where two independently derived models are in agreement with one another, and with solid‐state nuclear magnetic resonance (NMR) data. Simulations based on channel models may yield insights into possible ion conduction and selectivity mechanisms. BioEssays 20:992–1000, 1998. © 1998 John Wiley & Sons, Inc.