The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.

@article{Berrou2005TheCR,
  title={The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.},
  author={Laurent Berrou and Yolaine Dodier and Alexandra Raybaud and Audrey Tousignant and Omar Dafi and Joelle N Pelletier and Lucie Parent},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 1},
  pages={494-505}
}
The alpha-interacting domain (AID) in the I-II linker of high voltage-activated (HVA) Ca(2+) channel alpha1 subunits binds with high affinity to Ca(V)beta auxiliary subunits. The recently solved crystal structures of the AID-Ca(V)beta complex in Ca(V)1.1/1.2 have revealed that this interaction occurs through a set of six mostly invariant residues Glu/Asp(6), Leu(7), Gly(9), Tyr(10), Trp(13), and Ile(14) (where the superscript refers to the position of the residue starting with the QQ signature… CONTINUE READING

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