Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 전하정 | - |
dc.date.accessioned | 2019-12-05T14:51:47Z | - |
dc.date.available | 2019-12-05T14:51:47Z | - |
dc.date.issued | 2018-02 | - |
dc.identifier.citation | PHARMACOLOGICAL RESEARCH, v. 128, page. 211-219 | en_US |
dc.identifier.issn | 1043-6618 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/abs/pii/S104366181730703X?via%3Dihub | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/117580 | - |
dc.description.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 beta-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. | en_US |
dc.description.sponsorship | This work was supported by the biomedical technology development project, National Research Foundation, KOREA [NRF-2015M3A9B5030302 to SER]. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | en_US |
dc.subject | Dual specificity phosphatase | en_US |
dc.subject | Conformational switch | en_US |
dc.subject | Allosteric drug | en_US |
dc.subject | Structural intermediate | en_US |
dc.title | Two intermediate states of the conformational switch in dual specificity phosphatase 13a | en_US |
dc.type | Article | en_US |
dc.relation.volume | 128 | - |
dc.identifier.doi | 10.1016/j.phrs.2017.10.006 | - |
dc.relation.page | 211-219 | - |
dc.relation.journal | PHARMACOLOGICAL RESEARCH | - |
dc.contributor.googleauthor | Wei, Chun Hwa | - |
dc.contributor.googleauthor | Min, Hee Gyeong | - |
dc.contributor.googleauthor | Kim, Myeongbin | - |
dc.contributor.googleauthor | Kim, Gwan Hee | - |
dc.contributor.googleauthor | Chun, Ha-Jung | - |
dc.contributor.googleauthor | Ryu, Seong Eon | - |
dc.relation.code | 2018000914 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF MEDICINE[S] | - |
dc.sector.department | DEPARTMENT OF MEDICINE | - |
dc.identifier.pid | rthcchun | - |
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