2fys
From Proteopedia
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Crystal structure of Erk2 complex with KIM peptide derived from MKP3
Overview
Mitogen-activated protein (MAP) kinases are central components of signal, transduction pathways for cell proliferation, stress responses, and, differentiation. Signaling efficiency and specificity are modulated in, large part by docking interactions between individual MAP kinase and the, kinase interaction motif (KIM), (R/K)(2-3)-X(1-6)-Phi(A)-X-Phi(B), in its, cognate kinases, phosphatases, scaffolding proteins, and substrates. We, have determined the crystal structure of extracellular signal-regulated, protein kinase 2 bound to the KIM peptide from MAP kinase phosphatase 3, an extracellular signal-regulated protein kinase 2-specific phosphatase., The structure reveals that the KIM docking site, situated in a, noncatalytic region opposite of the kinase catalytic pocket, is comprised, of a highly acidic patch and a hydrophobic groove, which engage the basic, and Phi(A)-X-Phi(B) residues, respectively, in the KIM sequence. The, specific docking interactions observed in the structure consolidate all, known biochemical data. In addition, structural comparison indicates that, the KIM docking site is conserved in all MAP kinases. The results, establish a structural model for understanding how MAP kinases interact, with their regulators and substrates and provide new insights into how MAP, kinase docking specificity can be achieved.
About this Structure
2FYS is a Protein complex structure of sequences from Rattus norvegicus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3., Liu S, Sun JP, Zhou B, Zhang ZY, Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5326-31. Epub 2006 Mar 27. PMID:16567630
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