Role of Hydrophobic Residues in the C1b Domain of Protein Kinase C δ on Ligand and Phospholipid Interactions

Journal of Biological Chemistry

Volumn 276, Issue 22, 2001, Pages 19580-19587

  Wang, Qiming J ^a   Fang, Tzan Wei ^a   Nacro, Kassoum ^b   Marquez, Victor E ^b   Wang, Shaomeng ^c   Blumberg, Peter M ^a,b  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c GEORGETOWN UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ESTERS; HYDROPHOBICITY; MUTAGENESIS; PHOSPHOLIPIDS;

LIGANDS; MUTATIONS;

ENZYMES;

DIACYLGLYCEROL; LEUCINE; LIGAND; LYSINE; PHORBOL DIBUTYRATE; PHORBOL ESTER; PHOSPHOLIPID; PROTEIN KINASE C DELTA; ARGININE; CYSTEINE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; ISOENZYME; ISOPROTEIN; PROTEIN KINASE C; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING KINETICS; ESCHERICHIA COLI; GENE MUTATION; HYDROPHOBICITY; LIPID ANALYSIS; LIPID COMPOSITION; LIPOPHILICITY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LIPID INTERACTION; PROTEIN PURIFICATION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; ENZYMOLOGY; KINETICS; LIPID METABOLISM; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI; NEGIBACTERIA;

AMINO ACID SEQUENCE; ARGININE; CYSTEINE; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; GLUTATHIONE TRANSFERASE; ISOENZYMES; KINETICS; LEUCINE; LIGANDS; LIPID METABOLISM; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHORBOL ESTERS; PHOSPHOLIPIDS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN KINASE C; PROTEIN KINASE C-DELTA; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TYROSINE;

EID: 0035377312     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010089200     Document Type: Article

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