Ca2+ -sensitive inactivation and facilitation of L-type Ca2+ channels both depend on specific amino acid residues in a consensus calmodulin-binding motif in theα(1C) subunit

Journal of Biological Chemistry

Volumn 275, Issue 28, 2000, Pages 21121-21129

  Zühlke, Roger D ^a   Pitt, Geoffrey S ^b   Tsien, Richard W ^b   Reuter, Harald ^a  

^a UNIVERSITY OF BERN   (Switzerland)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CALCIUM ION; CALMODULIN; ISOLEUCINE; MUTANT PROTEIN; PROTEIN SUBUNIT; CALCIUM; CALCIUM CHANNEL L TYPE; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CALCIUM TRANSPORT; CONSENSUS SEQUENCE; CONTROLLED STUDY; FACILITATION; GENE OVEREXPRESSION; HYDROPHOBICITY; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN INTERACTION; XENOPUS; AMINO ACID SEQUENCE; BINDING SITE; CHEMISTRY; FIBROBLAST; GENETICS; HUMAN; KINETICS; MACROMOLECULE; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CALCIUM; CALCIUM CHANNELS, L-TYPE; CALMODULIN; CONSENSUS SEQUENCE; FIBROBLASTS; HUMANS; KINETICS; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS;

EID: 0034647344     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M002986200     Document Type: Article

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