Minimal determinants for binding activated Gα from the structure of a Gαil-peptide dimer

Biochemistry

Volumn 45, Issue 38, 2006, Pages 11390-11400

  Johnston, Christopher A ^a   Lobanova, Ekaterina S ^b   Shavkunov, Alexander S ^b   Low, Justin ^a   Ramer, J Kevin ^c,d   Blaesius, Rainer ^c,e   Fredericks, Zoey ^c,f   Willard, Francis S ^a   Kuhlman, Brian ^a   Arshavsky, Vadim Y ^b   Siderovski, David P ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b DUKE UNIVERSITY   (United States)

^c Karo Bio USA   (United States)

^d Entegrion   (United States)

^e Becton Dickinson Technologies   (United States)

^f AMGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOCHEMICAL ENGINEERING; DIMERS; HYDROPHOBICITY; MOLECULAR STRUCTURE; REACTION KINETICS;

CELLULAR SIGNALING; GOTRANSDUCIN; STRUCTURAL ANALYSES;

PROTEINS;

ALUMINUM DERIVATIVE; ALUMINUM TETRAFLUORIDE; BINDING PROTEIN; CYCLIC GMP; DIMER; FLUORIDE; GROWTH ASSOCIATED PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; KB 1753; PEPTIDE; PEPTIDE DERIVATIVE; PHOSPHODIESTERASE; RGS PROTEIN; TRANSDUCIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN VARIANT; STRUCTURE ANALYSIS;

ALUMINUM COMPOUNDS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; FLUORIDES; GTP-BINDING PROTEIN ALPHA SUBUNITS, GI-GO; GUANOSINE DIPHOSPHATE; HUMANS; LUMINESCENT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; RGS PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33749012581     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0613832     Document Type: Article

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