Structural highlights
3aln is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 3alo |
| 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matsumoto T, Kinoshita T, Kirii Y, Yokota K, Hamada K, Tada T. Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state. Biochem Biophys Res Commun. 2010 Sep 24;400(3):369-73. Epub 2010 Aug 21. PMID:20732303 doi:10.1016/j.bbrc.2010.08.071
