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- W2759496688 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." @default.
- W2759496688 created "2017-10-06" @default.
- W2759496688 creator A5056704911 @default.
- W2759496688 date "2018-02-01" @default.
- W2759496688 modified "2023-09-26" @default.
- W2759496688 title "Arenobufagin: A potential novel opportunity for prostate cancer treatment – Intriguing mechanistic data but some questions on in vivo translatability" @default.
- W2759496688 cites W2734348546 @default.
- W2759496688 doi "https://doi.org/10.1016/j.phrs.2017.09.015" @default.
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