Interaction of amiloride and one of its derivatives with Vpu from HIV‐1: a molecular dynamics simulation

FEBS Letters

Watts, A¹  Kim, C.G¹  Fischer, W.B¹  Ali, R¹  Lemaitre, V¹ 

[1]Biomembrane Structure Unit, Department of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK

关键词: Viral ion channel;    Vpu;    HIV-1;    Molecular dynamics simulation;    Drug–protein interaction;   

DOI  :  10.1016/S0014-5793(04)00251-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Vpu is an 81-residue membrane protein, with a single transmembrane segment that is encoded by HIV-1 and is involved in the enhancement of virion release via formation of an ion channel. Cyclohexamethylene amiloride (Hma) has been shown to inhibit ion channel activity. In the present 12-ns simulation study a putative binding site of Hma blockers in a pentameric model bundle built of parallel aligned helices of the first 32 residues of Vpu was found near Ser-23. Hma orientates along the channel axis with its alkyl ring pointing inside the pore, which leads to a blockage of the pore.

【 授权许可】

Unknown