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Vpu, an integral membrane protein encoded in HIV-1, is implicated in the release of new virus particles from infected cells, presumably mediated by ion channel activity of homo-oligomeric Vpu bundles. Reconstitution of both full length Vpu(1-81) and a short, the transmembrane (TM) domain comprising peptide Vpu(1-32) into bilayers under a constant electric field results in an asymmetric orientation of those channels. For both cases, channel activity with similar kinetics is observed. Channels can open and remain open within a broad series of conductance states even if a small or no electric potential is applied. The mean open time for Vpu peptide channels is voltage-independent. The rate of channel opening shows a biphasic voltage activation, implicating that the gating is influenced by the interaction of the dipole moments of the TM helices with an electric field.

Original publication

DOI

10.1080/07391102.2007.10507148

Type

Journal article

Journal

J Biomol Struct Dyn

Publication Date

06/2007

Volume

24

Pages

589 - 596

Keywords

Amino Acid Sequence, Electric Conductivity, HIV-1, Human Immunodeficiency Virus Proteins, Ion Channel Gating, Ion Channels, Kinetics, Molecular Sequence Data, Peptide Fragments, Recombinant Fusion Proteins, Viral Regulatory and Accessory Proteins