Simulation of the HIV‐1 Vpu transmembrane domain as a pentameric bundle

FEBS Letters

Klein, Michael L¹  Zhong, Qingfeng¹  Moore, Preston B¹  Husslein, Thomas¹ 

[1] Center for Molecular Modeling and Department of Chemistry, University of Pennsylvania, 231 S. 34th St., Philadelphia, PA 19104-6323, USA

关键词: Human immunodeficiency virus-1;    Vpu;    Transmembrane helix;    Ion channel;    Molecular dynamics;   

DOI  :  10.1016/S0014-5793(98)00714-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The transmembrane domain of oligomeric protein Vpu encoded by HIV-1 has been studied by means of a molecular dynamics simulation. A pentameric bundle of unconstrained helices (residues 6–28 of Vpu) with a water filled pore was initially assembled in a membrane mimetic octane/water system. This system was simulated, using the CHARMm19 and OPLS united atom force fields with no constraints at a temperature of 300 K and a pressure of 1 atm. For these forcefields and the initial conditions tested, the oligomeric bundle expelled most of the pore water molecules. The resulting bundle and residual waters adopt a conical structural motif with some resemblance to a potassium channel.

【 授权许可】

Unknown