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Ion channels formed by HIV‐1 Vpu: a modelling and simulation study
Author(s) -
Grice A.L,
Kerr I.D,
Sansom M.S.P
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00198-1
Subject(s) - ion channel , conductance , transmembrane protein , transmembrane domain , ion , protein subunit , chemistry , molecular dynamics , helix (gastropod) , crystallography , membrane , biophysics , chemical physics , physics , computational chemistry , biology , biochemistry , gene , condensed matter physics , ecology , receptor , organic chemistry , snail
Vpu is an oligomeric integral membrane protein encoded by HIV‐1 which forms ion channels, each subunit of which contains a single transmembrane helix. Models of Vpu channels formed by bundles of N =4, 5 or 6 transmembrane helices have been developed by restrained molecular dynamics and refined by 100 ps simulations with water molecules within the pore. Pore radius profiles and conductance predictions suggest that the N =5 model corresponds to the predominant channel conductance level of the channel. Potential energy profiles for translation of Na + or Cl − ions along the Vpu N =5 pore are consistent with the weak cation selectivity of Vpu channels.