2JFM

CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE (UNLIGANDED FORM)

Summary for 2JFM

• Entry DOI: 10.2210/pdb2jfm/pdb
• Related: 2J51 2JA0 2JFL
• Descriptor: STE20-LIKE SERINE-THREONINE KINASE, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: transferase, serine/threonine-protein kinase, atp-binding, phosphorylation, muscle development, kinase, apoptosis, germinal centre kinase, serine- threonine kinase 2, nucleotide-binding, serine-threonine-protein kinase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm : Q9H2G2
• Total number of polymer chains: 1
• Total formula weight: 37366.19

Authors

Pike, A.C.W.,Rellos, P.,Fedorov, O.,Keates, T.,Salah, E.,Savitsky, P.,Papagrigoriou, E.,Bunkoczi, G.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.,Weigelt, J.,Sundstrom, M.,Knapp, S. (deposition date: 2007-02-02, release date: 2007-02-27, Last modification date: 2018-01-24)

Primary citation

Pike, A.C.W.,Rellos, P.,Niesen, F.H.,Turnbull, A.,Oliver, A.W.,Parker, S.A.,Turk, B.E.,Pearl, L.H.,Knapp, S.
Activation Segment Dimerization: A Mechanism for Kinase Autophosphorylation of Non-Consensus Sites.
Embo J., 27:704-, 2008

PubMed Abstract: Protein kinase autophosphorylation of activation segment residues is a common regulatory mechanism in phosphorylation-dependent signalling cascades. However, the molecular mechanisms that guarantee specific and efficient phosphorylation of these sites have not been elucidated. Here, we report on three novel and diverse protein kinase structures that reveal an exchanged activation segment conformation. This dimeric arrangement results in an active kinase conformation in trans, with activation segment phosphorylation sites in close proximity to the active site of the interacting protomer. Analytical ultracentrifugation and chemical cross-linking confirmed the presence of dimers in solution. Consensus substrate sequences for each kinase showed that the identified activation segment autophosphorylation sites are non-consensus substrate sites. Based on the presented structural and functional data, a model for specific activation segment phosphorylation at non-consensus substrate sites is proposed that is likely to be common to other kinases from diverse subfamilies.

PubMed: 18239682
DOI: 10.1038/EMBOJ.2008.8

Experimental method

X-RAY DIFFRACTION (2.85 Å)