Modelling of the III-IV loop, a domain involved in calcium channel Cav2.1 inactivation, highlights a structural homology with the γ subunit of G proteins

European Journal of Neuroscience

Volumn 16, Issue 2, 2002, Pages 219-228

  Fathallah, Mohamed ^a,b   Sandoz, Guillaume ^b   Mabrouk, Kamel ^a   Geib, Sandrine ^b   Urbani, Julie ^b   Villaz, Michel ^b   Ronjat, Michel ^b   Sabatier, Jean Marc ^a   De Waard, Michel ^b  

^a CNRS   (France)

^b INSERM   (France)

Author keywords

Calcium channel structure; G protein regulation; Voltage dependent inactivation; Xenopus oocytes

Indexed keywords

CALCIUM CHANNEL; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CALCULATION; CONTROLLED STUDY; HYPERPOLARIZATION; KINETICS; LIPID BILAYER; MOLECULAR MECHANICS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; SEQUENCE HOMOLOGY; STEADY STATE; X RAY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM CHANNELS, N-TYPE; CALCIUM SIGNALING; CELL MEMBRANE; DOSE-RESPONSE RELATIONSHIP, DRUG; FEMALE; HETEROTRIMERIC GTP-BINDING PROTEINS; MEMBRANE POTENTIALS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; NEURONS; OOCYTES; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SYNAPSES; SYNAPTIC TRANSMISSION; XENOPUS LAEVIS;

EID: 0036976766     PISSN: 0953816X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1460-9568.2002.02074.x     Document Type: Article

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