Effect of charge substitutions at residue his-142 on voltage gating of connexin43 channels.

@article{Shibayama2006EffectOC,
  title={Effect of charge substitutions at residue his-142 on voltage gating of connexin43 channels.},
  author={Junko Shibayama and Cristina Guti{\'e}rrez and Daniel Gonzalez and Fabien Kieken and Akiko Seki and Jesus Requena Carri{\'o}n and Paul L Sorgen and Steven M. Taffet and Luis C. Barrio and Mario Delmar},
  journal={Biophysical journal},
  year={2006},
  volume={91 11},
  pages={4054-63}
}
Previous studies indicate that the carboxyl terminal of connexin43 (Cx43CT) is involved in fast transjunctional voltage gating. Separate studies support the notion of an intramolecular association between Cx43CT and a region of the cytoplasmic loop (amino acids 119-144; referred to as "L2"). Structural analysis of L2 shows two alpha-helical domains, each with a histidine residue in its sequence (H126 and H142). Here, we determined the effect of H142 replacement by lysine, alanine, and glutamate… CONTINUE READING

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