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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.

Original publication

DOI

10.1016/S0014-5793(04)00251-0

Type

Journal article

Journal

FEBS Lett

Publication Date

09/04/2004

Volume

563

Pages

75 - 81

Keywords

Amiloride, Amino Acid Sequence, Binding Sites, Computer Simulation, Drug Interactions, HIV-1, Human Immunodeficiency Virus Proteins, Hydrogen Bonding, Ion Channels, Models, Chemical, Models, Molecular, Protein Structure, Secondary, Protons, Serine, Time Factors, Viral Regulatory and Accessory Proteins