The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation

EMBO Journal

Volumn 20, Issue 6, 2001, Pages 1425-1438

  Qiu, Hongfang ^a   Dong, Jinsheng ^a   Hu, Cuihua ^a   Francklyn, Christopher S ^b   Hinnebusch, Alan G ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b UNIVERSITY OF VERMONT   (United States)

Author keywords

Dimerization; eIF2 ; GCN2; kinase; Regulation; Translation

Indexed keywords

HISTIDINE TRANSFER RNA LIGASE; INITIATION FACTOR 2; MESSENGER RNA; PROTEIN GCN2; PROTEIN KINASE; TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; DIMERIZATION; ENZYME ACTIVATION; ESCHERICHIA COLI; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; RNA BINDING; RNA TRANSLATION; TRANSLATION REGULATION;

ALLOSTERIC REGULATION; BINDING SITES; DIMERIZATION; DNA MUTATIONAL ANALYSIS; ENZYME ACTIVATION; HISTIDINE-TRNA LIGASE; MODELS, GENETIC; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; RNA, TRANSFER;

ESCHERICHIA COLI;

EID: 0035869040     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.6.1425     Document Type: Article

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