3VUT: Crystal structures of non-phosphorylated MAP2K4

Citation:
Abstract
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.
PDB ID: 3VUTDownload
MMDB ID: 102684
PDB Deposition Date: 2012/7/5
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 3.5  Å
Source Organism:
Similar Structures:
Biological Unit for 3VUT: monomeric; determined by author
Molecular Components in 3VUT
Label Count Molecule
Protein (1 molecule)
1
Dual Specificity Mitogen-activated Protein Kinase Kinase 4(Gene symbol: MAP2K4)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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