Thermodynamic study of the binding of the tandem-SH2 domain of the Syk kinase to a dually phosphorylated ITAM peptide: Evidence for two conformers

Biochemistry

Volumn 38, Issue 16, 1999, Pages 5024-5033

  Grucza, Richard A ^a   Fütterer, Klaus ^a   Chan, Andrew C ^a   Waksman, Gabriel ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD3 ANTIGEN; PEPTIDE FRAGMENT; PROTEIN KINASE SYK; PROTEIN TYROSINE KINASE; RECEPTOR SUBUNIT; SODIUM CHLORIDE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

ARTICLE; BINDING KINETICS; ENTHALPY; IMMUNE RECEPTOR TYROSINE ACTIVATION MOTIF; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REACTION ANALYSIS; RECEPTOR AFFINITY; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE;

ANTIGENS, CD3; CIRCULAR DICHROISM; ENZYME PRECURSORS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; OLIGOPEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN-TYROSINE KINASES; RECEPTORS, AMINO ACID; RECEPTORS, ANTIGEN, T-CELL; SRC HOMOLOGY DOMAINS; TEMPERATURE; THERMODYNAMICS; TYROSINE;

EID: 0040799939     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9829938     Document Type: Article

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