Key result
Human Hv1 forms a dimer in the membrane with interfaces mediated by S1, the adjacent extracellular loop, and a putative intracellular coiled-coil domain.
Population
tsA201 cells (HEK293 derivatives) transfected with human Hv1 cDNAs
Design
Preclinical
Authors
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Hv1 dimer structure may guide inhibitor design; leaves open functional validation in human disease models.
Human Hv1 channels exist as dimers in the cell membrane, with interfaces at the extracellular S1 loop and intracellular coiled-coil domain, providing structural insights into voltage-gated proton channels.
Lee et al. (2008) studied this question. Cysteine cross-linking and mutagenesis was evaluated on Oligomeric state and dimer interface of Hv1. Human Hv1 forms a dimer in the membrane with interfaces mediated by S1, the adjacent extracellular loop, and a putative intracellular coiled-coil domain.
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