Publication Abstract from PubMed
p90 ribosomal S6 kinases (RSKs) respond to various mitogen stimuli and comprise two distinct protein kinase domains. The C-terminal kinase domain (CTKD) receives signal from ERK1/2 and adopts an autoinhibitory mechanism. Here, the crystal structure of human RSK1 CTKD is reported at 2.7 A resolution. The structure shows a standard kinase fold, with the catalytic residues in the ATP-binding cleft orientated in optimal conformations for phosphotransfer. The inactivation of the CTKD is conferred by an extra alpha-helix (alphaL), which occupies the substrate-binding groove. In combination with previous knowledge, this structure indicates that activation of RSK1 involves the removal of alphaL from the substrate-binding groove induced by ERK1/2 phosphorylation.
Structural basis for the autoinhibition of the C-terminal kinase domain of human RSK1.,Li D, Fu TM, Nan J, Liu C, Li LF, Su XD Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):680-5. Epub 2012 May 17. PMID:22683790[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
