The structure of the HIV-1 Vpu ion channel: modelling and simulation studies

被引：47

作者：

Cordes, FS

Kukol, A

Forrest, LR

Arkin, IT

Sansom, MSP

Fischer, WB

机构：

[1] Univ Oxford, Dept Biochem, Lab Mol Biophys, Oxford OX1 3QU, England

[2] Univ Cambridge, Dept Biochem, Cambridge Ctr Mol Recognit, Cambridge CB2 1GA, England

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2001年 / 1512卷 / 02期

基金：

英国惠康基金;

关键词：

HIV-1; Vpu; viral ion channel; molecular dynamics; gating;

D O I：

10.1016/S0005-2736(01)00332-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Vpu is an 81 amino acid auxiliary protein in HIV-1 which exhibits channel activity. We used two homo-pentameric bundles with the helical transmembrane segments derived from FTIR spectroscopy in combination with a global molecular dynamics search protocol: (i) tryptophans (W) pointing into the pore, and (ii) W facing the lipids. Two equivalent bundles have been generated using a simulated annealing via a restrained molecular dynamics simulations (SA/MD) protocol. A fifth model was generated via SA/MD with all serines facing the pore. The latter model adopts a very stable structure during the 2 ns of simulation. The stability of the models with W facing the pore depends on the starting structure. A possible gating mechanism is outlined. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：291 / 298

页数：8

共 57 条

[1] COMPUTATIONAL SEARCHING AND MUTAGENESIS SUGGEST A STRUCTURE FOR THE PENTAMERIC TRANSMEMBRANE DOMAIN OF PHOSPHOLAMBAN [J].