3alo | pdb_00003alo

Crystal structure of human non-phosphorylated MKK4 kinase domain ternary complex with AMP-PNP and p38 peptide

spinqualitylabelsall models 3alo, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3alo is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, MG NonStd Res: TPO Related: 3aln Gene: JNKK1, MAP2K4, MEK4, MKK4, PRKMK4, SERK1 (Homo sapiens) Activity: Mitogen-activated protein kinase kinase, with EC number 2.7.12.2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed MKK4 activates both JNKs and p38s. We determined the crystal structures of human non-phosphorylated MKK4 kinase domain (npMKK4) complexed with AMP-PNP (npMKK4/AMP) and a ternary complex of npMKK4, AMP-PNP and p38alpha peptide (npMKK4/AMP/p38). These crystal structures revealed that the p38alpha peptide-bound npMKK4 at the allosteric site rather than at the putative substrate binding site and induced an auto-inhibition state. While the activation loop of the npMKK4/AMP complex was disordered, in the npMKK4/AMP/p38 complex it configured a long alpha-helix, which prevented substrate access to the active site and alphaC-helix movement to the active configuration of MKK4. Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state.,Matsumoto T, Kinoshita T, Kirii Y, Yokota K, Hamada K, Tada T Biochem Biophys Res Commun. 2010 Sep 24;400(3):369-73. Epub 2010 Aug 21. PMID:20732303 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mitogen-activated protein kinase kinase

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