5XJV
Two intermediate states of conformation switch in dual specificity phosphatase 13a
Summary for 5XJV
| Entry DOI | 10.2210/pdb5xjv/pdb |
| Descriptor | Dual specificity protein phosphatase 13 isoform A, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | dusp13a, ptp, conformation switch, catalytic domain, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm : Q6B8I1 |
| Total number of polymer chains | 2 |
| Total formula weight | 40721.99 |
| Authors | Wei, C.H.,Min, H.G.,Chun, H.J.,Ryu, S.E. (deposition date: 2017-05-04, release date: 2018-04-11, Last modification date: 2023-11-22) |
| Primary citation | Wei, C.H.,Min, H.G.,Kim, M.,Kim, G.H.,Chun, H.J.,Ryu, S.E. Two intermediate states of the conformational switch in dual specificity phosphatase 13a Pharmacol. Res., 128:211-219, 2018 Cited by PubMed Abstract: Dual specificity phosphatases (DUSPs) include MAP kinase phosphatases and atypical dual specificity phosphatases and mediate cell growth and differentiation, brain function, and immune responses. They serve as targets for drug development against cancers, diabetes and depression. Several DUSPs have non-canonical conformation of the central β-sheet and active site loops, suggesting that they may have conformational switch that is related to the regulation of enzyme activity. Here, we determined the crystal structure of DUSP13a, and identified two different structures that represent intermediates of the postulated conformational switch. Amino acid sequence of DUSP13a is not significantly homologous to DUSPs with conformational switch, indicating that the conformational switch is not sequence-dependent, but rather determined by ligand interaction. The sequence-independency suggests that other DUSPs with canonical conformation may have the conformational switch during specific cellular regulation. The conformational switch leads to significant changes in the protein surface, including a hydrophobic surface and pockets, which can be exploited for development of allosteric modulators of drug target DUSPs. PubMed: 29106959DOI: 10.1016/j.phrs.2017.10.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.69 Å) |
Structure validation
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