Simulations of the BM2 proton channel transmembrane domain from influenza virus B.

Journal article

BM2 is a small integral membrane protein from influenza B virus which forms proton-permeable channels. Coarse-grained (CG) molecular dynamics simulations have been used to produce a model of the BM2 channel by self-assembly of a tetrameric bundle of BM2 transmembrane helices in a lipid bilayer. The BM2 channel model is conformationally stable on a 5 mus time scale. This CG model was converted to atomistic resolution to refine interhelix and channel-water interactions. Atomistic molecular dynamics simulations indicate that the BM2 channel is closed when no more than two of the four His19 residues are protonated. Protonating a third His19 side chain initiates a conformational change that opens the channel. In summary, our simulations suggest a common mechanism for BM2 and A/M2, whereby changes in helix packing play a functional role in channel gating.

Authors: Rouse, S; Carpenter, T; Stansfeld, P; Sansom, MS

• Publication status: Published
• Journal: Biochemistry
• Volume: 48
• Issue: 42
• Pages: 9949-9951
• Publication date: 2009-10-01
• DOI: 10.1021/bi901166n
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Influenza B virus; Protein Structure, Tertiary; Viral Proteins; Computer Simulation; Models, Molecular; Membrane Proteins