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Article

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

The Journal of biological chemistry - 7 Jan 2005

Berrou Laurent, Dodier Yolaine, Raybaud Alexandra, Tousignant Audrey, Dafi Omar, Pelletier Joelle N, Parent Lucie

Abstract excerpt

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...

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PMID: 15507442
DOI: 10.1074/jbc.M410859200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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