Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: A unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation

Journal of Biological Chemistry

Volumn 283, Issue 29, 2008, Pages 20569-20578

  Ishida, Hiroaki ^a   Borman, Meredith A ^b   Ostrander, Janina ^b   Vogel, Hans J ^a   MacDonald, Justin A ^a,c  

^a UNIVERSITY OF CALGARY   (Canada)

^b UNIVERSITY OF CALGARY   (Canada)

^c LIBIN CARDIOVASCULAR INSTITUTE OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CALCIUM; FLOW INTERACTIONS; MUSCLE; NUCLEAR MAGNETIC RESONANCE; PORT TERMINALS; PROTEINS; SURFACE STRUCTURE; VOLUMETRIC ANALYSIS;

BINDING LOOPS; BINDING MODES; BIOLOGICAL FUNCTIONS; C TERMINUSES; CALPONIN HOMOLOGIES; DISTINCT FEATURES; DO-MAINS; IN VITRO; ISOTHERMAL TITRATION CALORIMETRIES; NMR CHEMICAL SHIFT PERTURBATIONS; PROTEIN DOCKING; SECONDARY STRUCTURES; SEQUENCE IDENTITIES; SMOOTH MUSCLES; SOLUTION STRUCTURES; TERMINAL DOMAINS;

CAMS;

CALCIUM ION; CALMODULIN; CALPONIN; DOCKING PROTEIN; SMOOTHELIN LIKE 1 PROTEIN; SMOOTHENED PROTEIN; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; CALCIUM BINDING PROTEIN; CHASM PROTEIN, MOUSE; MUSCLE PROTEIN; PHOSPHOPROTEIN;

ALPHA HELIX; ARTICLE; BINDING KINETICS; BINDING SITE; CALCIUM BINDING; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; HUMAN; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR MODEL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE HOMOLOGY; SMOOTH MUSCLE RELAXATION; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CHICKEN; GENETICS; METABOLISM; MOLECULAR GENETICS; MUSCLE RELAXATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SMOOTH MUSCLE; STRUCTURAL HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM-BINDING PROTEINS; CALMODULIN; CALORIMETRY; CHICKENS; CONSERVED SEQUENCE; MICE; MICROFILAMENT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; MUSCLE RELAXATION; MUSCLE, SMOOTH; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 50649109020     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M800627200     Document Type: Article

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