This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3vut 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.
Mitogen-activated protein kinase kinase 4 (MAP2K4) plays a crucial role in the stress-activated signal cascade and is enzymatically regulated by ligand or substrate binding, and/or post-translational modification. Crystal structures combined with small-angle X-ray scattering experiments revealed that the apo form of non-phosphorylated MAP2K4 (npMAP2K4) exists in a transient state which has a longer conformation compared with the typical kinase folding. Upon ATP-binding, the transient conformation adopted the configuration of typical kinase folding. In the absence of ATP-binding, the transient state of apo npMAP2K4 may shift to a state of aggregation via non-particular hydrophobic interactions as a result of the exposed hydrophobic residues.
Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4.,Matsumoto T, Kinoshita T, Kirii Y, Tada T, Yamano A Biochem Biophys Res Commun. 2012 Aug 24;425(2):195-200. Epub 2012 Jul 22. PMID:22828509[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Matsumoto T, Kinoshita T, Kirii Y, Tada T, Yamano A. Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4. Biochem Biophys Res Commun. 2012 Aug 24;425(2):195-200. Epub 2012 Jul 22. PMID:22828509 doi:http://dx.doi.org/10.1016/j.bbrc.2012.07.066
