Structural insights into Ca2+-dependent regulation of inositol 1,4,5-trisphosphate receptors by CaBP1

Journal of Biological Chemistry

Volumn 284, Issue 4, 2009, Pages 2472-2481

  Li, Congmin ^a   Chan, Jenny ^b   Haeseleer, Franciose ^c   Mikoshiba, Katsuhiko ^d   Palczewski, Krzysztof ^e   Ikura, Mitsuhiko ^b   Ames, James B ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF TORONTO   (Canada)

^c UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^d RIKEN BRAIN SCIENCE INSTITUTE   (Japan)

^e CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; CAMS; SUGARS;

BOUND STATE; C DOMAINS; CALCIUM-BINDING PROTEINS; HYDROPHOBIC RESIDUES; ISOTHERMAL TITRATION CALORIMETRIES; LIGAND BINDINGS; N TERMINALS; NMR STRUCTURES; SELECTIVE BINDINGS; STRUCTURAL INSIGHTS; STRUCTURAL INTERACTIONS;

CALCIUM;

CALCIUM; CALCIUM BINDING PROTEIN; CALCIUM BINDING PROTEIN 1; HISTONE; HYBRID PROTEIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; ISOLEUCINE; LEUCINE; MAGNESIUM; MUTANT PROTEIN; UNCLASSIFIED DRUG; VALINE; CA2+ BINDING PROTEIN 1; CA2+-BINDING PROTEIN-1; CALMODULIN;

ARTICLE; BINDING AFFINITY; CALCIUM TRANSPORT; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CYTOSOL; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN MOTIF; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; CALCIUM; CALCIUM-BINDING PROTEINS; CALMODULIN; CYTOSOL; EF HAND MOTIFS; HUMANS; INOSITOL 1,4,5-TRISPHOSPHATE RECEPTORS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

EID: 59049101580     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M806513200     Document Type: Article

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