An α-helical C-terminal tail segment of the skeletal L-type Ca 2+ channel β1a subunit activates ryanodine receptor type 1 via a hydrophobic surface

FASEB Journal

Volumn 26, Issue 12, 2012, Pages 5049-5059

  Karunasekara, Yamuna ^a   Rebbeck, Robyn T ^a   Weaver, Llara M ^a   Board, Philip G ^a   Dulhunty, Angela F ^a   Casarotto, Marco G ^a  

^a Biology and Environment   (Australia)

Author keywords

Excitation contraction coupling; Protein protein interaction

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; AMINO ACID; BETA1A PEPTIDE; CALCIUM CHANNEL L TYPE; CARBOXY TERMINAL TELOPEPTIDE; RYANODINE RECEPTOR 1; UNCLASSIFIED DRUG;

ALPHA HELIX; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; EXCITATION CONTRACTION COUPLING; GENE MUTATION; HYDROPHOBICITY; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN BINDING; RABBIT; SKELETAL MUSCLE;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BINDING SITES; CALCIUM CHANNELS, L-TYPE; EXCITATION CONTRACTION COUPLING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RABBITS; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL; SEQUENCE HOMOLOGY, AMINO ACID; SURFACE PROPERTIES;

ORYCTOLAGUS CUNICULUS;

EID: 84870385652     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.12-211334     Document Type: Article

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