Phosphorylation- and nucleotide-binding-induced changes to the stability and hydrogen exchange patterns of JNK1β1 provide insight into its mechanisms of activation

Journal of Molecular Biology

Volumn 426, Issue 21, 2014, Pages 3569-3589

  Owen, Gavin R ^a   Stoychev, Stoyan ^b   Achilonu, Ikechukwu ^a   Dirr, Heini W ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

^b DSI CSIR Nanotechnology Innovation Centre   (South Africa)

Author keywords

c Jun N terminal kinase; hydrogen exchange; MAP kinases; mass spectrometry; protein dynamics

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; ADENYLYLIMIDODIPHOSPHATE; C JUN AMINO TERMINAL KINASE 1 BETA 1; MITOGEN ACTIVATED PROTEIN KINASE; SOLVENT; STRESS ACTIVATED PROTEIN KINASE 1; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; UREA; ADENOSINE TRIPHOSPHATE; HYDROGEN; MITOGEN ACTIVATED PROTEIN KINASE 10; NUCLEOTIDE; PROTEIN BINDING;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEUTERIUM HYDROGEN EXCHANGE; ENZYME ACTIVATION; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; HINGE REGION; LIGAND BINDING; MASS SPECTROMETRY; NONHUMAN; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TEMPERATURE; THERMOSTABILITY; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; ESCHERICHIA COLI; HUMAN; MOLECULAR GENETICS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SIGNAL TRANSDUCTION; THERMODYNAMICS;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; DEUTERIUM EXCHANGE MEASUREMENT; ENZYME ACTIVATION; ESCHERICHIA COLI; HUMANS; HYDROGEN; MAP KINASE SIGNALING SYSTEM; MASS SPECTROMETRY; MITOGEN-ACTIVATED PROTEIN KINASE 10; MITOGEN-ACTIVATED PROTEIN KINASE 8; MOLECULAR SEQUENCE DATA; NUCLEOTIDES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SOLVENTS; TEMPERATURE; THERMODYNAMICS; UREA;

EID: 84907855417     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.08.019     Document Type: Article

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