ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Expression, purification, crystallization and preliminary crystallographic study of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Spectrum and functions of ion channels and transporters in osteoclasts.Bone research · 2026Review
- Proton pump inhibitors have pH-dependent effects on the thermostability of the carboxyl-terminal domain of voltage-gated proton channel Hv1.European biophysics journal : EBJ · 2018Article
- Detergent screening of the human voltage-gated proton channel using fluorescence-detection size-exclusion chromatography.Protein science : a publication of the Protein Society · 2014Article
- Human voltage-gated proton channel hv1: a new potential biomarker for diagnosis and prognosis of colorectal cancer.PloS one · 2013Article
- Clinicopathological and biological significance of human voltage-gated proton channel Hv1 protein overexpression in breast cancer.The Journal of biological chemistry · 2012Article
- Zinc inhibition of monomeric and dimeric proton channels suggests cooperative gating.The Journal of physiology · 2010Article
- The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.The Journal of biological chemistry · 2010Article
- Architecture and gating of Hv1 proton channels.The Journal of physiology · 2009Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The voltage-gated proton channel Hv1 is essential to proton permeation and contains a voltage-sensor domain without a pore domain. It contains three predicted domains: an N-terminal acid and proline-rich domain, a transmembrane voltage-sensor domain and a C-terminal domain that is responsible for the dimeric architecture of Hv1. Here, the C-terminal domain of the human voltage-gated proton channel Hv1 (C-Hv1) was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals have a tetragonal form and diffraction data were collected to 2.5 A resolution in-house. The crystal belongs to space group P4(1)2(1)2, with unit-cell parameters a = b = 37.76, c = 137.52 A. Structural determination of C-Hv1 is in progress.
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