The structure of the PERK kinase domain suggests the mechanism for its activation

Acta Crystallographica Section D: Biological Crystallography

Volumn 67, Issue 5, 2011, Pages 423-428

  Cui, Wenjun ^a   Li, Jingzhi ^a   Ron, David ^b   Sha, Bingdong ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

eIF2 kinase; endoplasmic reticulum; kinase domains; PERK; protein translation; UPR

Indexed keywords

PERK KINASE; PROTEIN KINASE R;

ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; METABOLISM; MOUSE; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE; SIGNAL TRANSDUCTION; UNFOLDED PROTEIN RESPONSE; X RAY CRYSTALLOGRAPHY;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; EIF-2 KINASE; ENZYME ACTIVATION; MICE; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; SIGNAL TRANSDUCTION; UNFOLDED PROTEIN RESPONSE;

EID: 79955656979     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444911006445     Document Type: Article

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