Structural modes of stabilization of permissive phosphorylation sites in protein kinases: Distinct strategies in Ser/Thr and Tyr kinases

Journal of Molecular Biology

Volumn 339, Issue 5, 2004, Pages 1025-1039

  Krupa, A ^a   Preethi, G ^b   Srinivasan, N ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b BHARATHIAR UNIVERSITY   (India)

Author keywords

active and inactive state; CK2, casein kinase 2; GS, glycine serine; GSK, glycogen synthase kinase; GSK 3, glycogen synthase kinase 3; phosphorylation; PKA, protein kinase A; PKB, protein kinase B; protein kinase; regulation; stabilization of active site

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; ARGININE; CASEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLUTAMINE; GLYCINE; GLYCOGEN SYNTHASE KINASE 3BETA; HISTIDINE; HYDROXYL GROUP; LEUCINE; LYSINE; MAGNESIUM; MANGANESE; MITOGEN ACTIVATED PROTEIN KINASE; PHENYLALANINE; PHOSPHATE; PHOSPHOAMINO ACID; PHOSPHOTHREONINE; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE; RIBOSE; THREONINE; TRANSFORMING GROWTH FACTOR BETA; VALINE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ATOM; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; ENZYME ACTIVATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; PROTEIN-TYROSINE KINASES; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION;

EID: 3042584697     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.043     Document Type: Review

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