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Insight into the Role of the Hv1 C-Terminal Domain in Dimer Stabilization

The voltage-gated proton-selective channel (Hv1) conducts protons in response to changes in membrane potential. The Hv1 protein forms dimers in the membrane. Crystal structures of Hv1 channels have revealed that the primary contacts between the two monomers are in the C-terminal domain (CTD), which forms a coiled-coil structure. The role of Hv1-CTD in channel assembly and activity is not fully understood. Here, molecular dynamics (MD) simulations of full-length and truncated CTD models of human and mouse Hv1 channels reveal a strong contribution of the CTD to the packing of the transmembrane domains. Simulations of the CTD models highlight four fundamental interactions of the key residues contributing to dimer stability. These include salt bridges, hydrophobic interactions, hydrogen bonds, and a disulfide bond across the dimer interface. At neutral pH, salt-bridge interactions increase dimer stability and the dimer becomes less stable at acidic pH. Hydrophobic core packing of the heptad pattern is importa...

Authors:   Panisak Boonamnaj; Pornthep Sompornpisut
Journal:   Journal of Physical Chemistry B
Year:   2018
DOI:   10.1021/acs.jpcb.7b08669
Publication date:   16-Jan-2018
Facts, background information, dossiers
  • interactions
  • molecular dynamics
  • stability
  • hydrogen bonds
  • crystal structures
More about American Chemical Society Publications
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