 |
PDBsum entry 3a2a
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
3a2a
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The role and structure of the carboxyl-Terminal domain of the human voltage-Gated proton channel hv1.
|
|
|
Authors
|
|
S.J.Li,
Q.Zhao,
Q.Zhou,
H.Unno,
Y.Zhai,
F.Sun.
|
|
|
Ref.
|
|
J Biol Chem, 2010,
285,
12047-12054.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
