Multiple Activation Loop Conformations and Their Regulatory Properties in the Insulin Receptor's Kinase Domain

Journal of Biological Chemistry

Volumn 276, Issue 50, 2001, Pages 46933-46940

  Ablooglu, Ararat J ^a   Frankel, Mark ^d   Rusinova, Elena ^d   Ross, John B Alexander ^b   Kohanski, Ronald A ^c  

^a GEOPHYSICAL LABORATORY   (United States)

^b UNIVERSITY OF MONTANA   (United States)

^c MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^d NONE

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CONFORMATIONS; ENZYME KINETICS; MUTAGENESIS;

MUTATIONS;

ENZYMES;

ARGININE; ASPARAGINE; GLYCINE; INSULIN RECEPTOR KINASE; LYSINE; TYROSINE; ADENOSINE DIPHOSPHATE; ASPARTIC ACID; COMPLEMENTARY DNA; INSULIN RECEPTOR; PEPTIDE;

ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; FLUORESCENCE; HORMONE RECEPTOR INTERACTION; INHIBITION KINETICS; NONHUMAN; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STEADY STATE; STEREOCHEMISTRY; ANIMAL; BINDING SITE; BIOLOGICAL MODEL; CHEMISTRY; ENZYME SPECIFICITY; HYDROGEN BOND; KINETICS; METABOLISM; MOLECULAR CLONING; MUTATION; PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; RAT; SITE DIRECTED MUTAGENESIS; SPECTROFLUOROMETRY; TIME;

ADENOSINE DIPHOSPHATE; ANIMAL; ARGININE; ASPARTIC ACID; BINDING SITES; CATALYSIS; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN BONDING; KINETICS; MODELS, BIOLOGICAL; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTOR, INSULIN; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, P.H.S.; TIME FACTORS; TYROSINE;

EID: 0035861673     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M107236200     Document Type: Article

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