3VUT
Crystal structures of non-phosphorylated MAP2K4
Summary for 3VUT
| Entry DOI | 10.2210/pdb3vut/pdb |
| Descriptor | Dual specificity mitogen-activated protein kinase kinase 4 (1 entity in total) |
| Functional Keywords | apo form, kinase, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : P45985 |
| Total number of polymer chains | 2 |
| Total formula weight | 74941.99 |
| Authors | Matsumoto, T.,Kinoshita, T.,Kirii, Y.,Tada, T.,Yamano, A. (deposition date: 2012-07-05, release date: 2012-09-05, Last modification date: 2024-03-20) |
| Primary citation | 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., 425:195-200, 2012 Cited by PubMed 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. PubMed: 22828509DOI: 10.1016/j.bbrc.2012.07.066 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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