Autoinhibitory interdomain interactions and subfamilyspecific extensions redefine the catalytic core of the human DEAD-box protein DDX3

Journal of Biological Chemistry

Volumn 291, Issue 5, 2016, Pages 2412-2421

  Floor, Stephen N ^a   Condon, Kendall J ^a   Sharma, Deepak ^b   Jankowsky, Eckhard ^b   Doudna, Jennifer A ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; RNA;

C-TERMINAL DOMAINS; CATALYTIC CORE; HUMAN MALIGNANCIES; INTER-DOMAIN INTERACTIONS; MEDULLOBLASTOMA; PROTEIN TRANSLATION; RNA BINDING SURFACE; RNA-PROTEIN COMPLEXES;

PROTEINS;

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; DEAD BOX PROTEIN; DEAD BOX PROTEIN DDX3; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; DDX3X PROTEIN, HUMAN; RECA PROTEIN; RECOMBINANT PROTEIN; RNA;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; MOLECULAR CLONING; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN SYNTHESIS; RNA BINDING; SEQUENCE ALIGNMENT; ANIMAL; CHEMISTRY; DROSOPHILA MELANOGASTER; ENZYME ACTIVE SITE; GENE EXPRESSION REGULATION; GENETIC COMPLEMENTATION; HUMAN; MEDULLOBLASTOMA; METABOLISM; MOUSE; MUTATION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES; X RAY CRYSTALLOGRAPHY; ZEBRA FISH;

ADENOSINE TRIPHOSPHATASES; ANIMALS; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DEAD-BOX RNA HELICASES; DROSOPHILA MELANOGASTER; GENE EXPRESSION REGULATION; GENETIC COMPLEMENTATION TEST; HUMANS; MEDULLOBLASTOMA; MICE; MOLECULAR DYNAMICS SIMULATION; MUTATION; PROTEIN STRUCTURE, TERTIARY; REC A RECOMBINASES; RECOMBINANT PROTEINS; RNA; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES; ZEBRAFISH;

EID: 84957026340     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.700625     Document Type: Article

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