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X-ray crystal structure of voltage-gated proton channel
- K. Takeshita, Souhei Sakata, +8 authors A. Nakagawa
- Chemistry, MedicineNature Structural &Molecular Biology
- 1 April 2014
A crystal structure of mouse Hv1 in the resting state showing a 'closed umbrella' shape with a long helix consisting of the cytoplasmic coiled coil and the voltage-sensing helix, S4, and featured a wide inner-accessible vestibule provides a platform for understanding the general principles of voltage sensing and proton permeation.
Regulation of the desensitization and ion selectivity of ATP‐gated P2X2 channels by phosphoinositides
Results show that membrane‐bound PIPns play a key role in maintaining channel activity and regulating pore dilation through electrostatic interaction with the proximal region of the P2X2 cytoplasmic C‐terminal domain.
Structural Insights into Divalent Cation Modulations of ATP-Gated P2X Receptor Channels.
The crystal structure of an invertebrate P2X receptor from the Gulf Coast tick Amblyomma maculatum in the presence of ATP and Zn(2+) ion is reported, together with electrophysiological and computational analyses, and provides structural insights into the divalent cation modulations of P2x receptors.
The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H(+) channel Hv1.
- Y. Fujiwara, Tatsuki Kurokawa, +4 authors Y. Okamura
- Chemistry, MedicineNature communications
- 8 May 2012
The results indicate that the cytoplasmic coiled-coil strands form continuous α-helices with S4 and mediate cooperative gating to adjust the range of temperatures over which Hv1/VSOP operates.
Selection of Inhibitor-Resistant Viral Potassium Channels Identifies a Selectivity Filter Site that Affects Barium and Amantadine Block
The data support the idea that permeant ions have an integral role in stabilizing potassium channel structure, suggest that both barium and amantadine act at a similar site, and demonstrate how genetic selections can be used to map blocker binding sites and reveal mechanistic features.
Structures of CaV2 Ca2+/CaM-IQ domain complexes reveal binding modes that underlie calcium-dependent inactivation and facilitation.
- E. Y. Kim, C. Rumpf, Y. Fujiwara, E. S. Cooley, F. van Petegem, D. Minor
- Chemistry, MedicineStructure
- 8 October 2008
The data unveil the remarkable structural plasticity at the heart of Ca(V) feedback modulation and indicate that Ca (V)1 and Ca( V)2 IQ domains bear a dedicated CDF site that exchanges Ca(2+)/CaM lobe occupants.
Functional Roles of Charged Amino Acid Residues on the Wall of the Cytoplasmic Pore of Kir2.1
It is known that rectification of currents through the inward rectifier K+ channel (Kir) is mainly due to blockade of the outward current by cytoplasmic Mg2+ and polyamines. Analyses of the crystal…
Density‐dependent changes of the pore properties of the P2X2 receptor channel
The pore properties of P2X2 channel are not static but change dynamically depending on the open channel density, and it is identified by mutagenesis study that Ile328 located at the outer mouth of the pore is critical for the density‐dependent changes of P 2X2.
Long α helices projecting from the membrane as the dimer interface in the voltage-gated H+ channel
- Y. Fujiwara, Tatsuki Kurokawa, Y. Okamura
- Chemistry, MedicineThe Journal of general physiology
- 1 March 2014
Continuous helices extending from the transmembrane region to the cytoplasmic region form a dimeric interface to regulate activation of the voltage-gated H+ channel.
Novel KCNJ2 Mutation in Familial Periodic Paralysis With Ventricular Dysrhythmia
T192, which is located in the phosphatidylinositol-4,5-bisphosphate binding site and also the region necessary for Kir2.1 multimerization, is a highly conserved amino acid residue among inward-rectifier channels.