Article
Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2.
The Journal of biological chemistry - 12 Aug 2005
Padyana Anil K, Qiu Hongfang, Roll-Mecak Antonina, Hinnebusch Alan G, Burley Stephen K
Abstract excerpt
The GCN2 protein kinase coordinates protein synthesis with levels of amino acid stores by phosphorylating eukaryotic translation initiation factor 2. The autoinhibited form of GCN2 is activated in cells starved of amino acids by binding of uncharged tRNA to a histidyl-tRNA synthetase-like domain. Replacement of Arg-794 with Gly in the PK domain (R794G) activates GCN2 independently of tRNA binding. Crystal...
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