3A2A

The structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1

3A2A の概要

• エントリーDOI: 10.2210/pdb3a2a/pdb
• 分子名称: Voltage-gated hydrogen channel 1, CHLORIDE ION (3 entities in total)
• 機能のキーワード: voltage-gated proton channel, alternative splicing, coiled coil, ion transport, ionic channel, membrane, transmembrane, transport, voltage-gated channel, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Multi-pass membrane protein: Q96D96
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 26905.99

構造登録者

Li, S.J.,Unno, H.,Zhou, Q.,Zhao, Q.,Zhai, Y.,Sun, F. (登録日: 2009-05-08, 公開日: 2010-02-09, 最終更新日: 2024-10-23)

主引用文献

Li, S.J.,Zhao, Q.,Zhou, Q.,Unno, H.,Zhai, Y.,Sun, F.
The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.
J.Biol.Chem., 285:12047-12054, 2010

PubMed Abstract: The voltage-gated proton channel Hv1 has a voltage sensor domain but lacks a pore domain. Although the C-terminal domain of Hv1 is known to be responsible for dimeric architecture of the channel, its role and structure are not known. We report that the full-length Hv1 is mainly localized in intracellular compartment membranes rather than the plasma membrane. Truncation of either the N or C terminus alone or both together revealed that the N-terminal deletion did not alter localization, but deletion of the C terminus either alone or together with the N terminus resulted in expression throughout the cell. These results indicate that the C terminus is essential for Hv1 localization but not the N terminus. In the 2.0 A structure of the C-terminal domain, the two monomers form a dimer via a parallel alpha-helical coiled-coil, in which one chloride ion binds with the Neta atom of Arg(264). A pH-dependent structural change of the protein has been observed, but it remains a dimer irrespective of pH value.

PubMed: 20147290
DOI: 10.1074/jbc.M109.040360

実験手法

X-RAY DIFFRACTION (2 Å)