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