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- Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms
- Dae Gwin Jeong; Seung-Jun Kim; J H Kim; Jeong Hee Son; Mi Rim Park; Sang Myoun Lim; Tae-Sung Yoon; Seong Eon Ryu
- Bibliographic Citation
- Journal of Molecular Biology, vol. 345, no. 2, pp. 401-413
- Publication Year
- The PRL phosphatases, which constitute a subfamily of the protein tyrosine phosphatases (PTPs), are implicated in oncogenic and metastatic processes. Here, we report the crystal structure of human PRL-1 determined at 2.7 ? resolution. The crystal structure reveals the shallow active-site pocket with highly hydrophobic character. A structural comparison with the previously determined NMR structure of PRL-3 exhibits significant differences in the active-site region. In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site. We also found that PRL-1 forms a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL-1 activity by oligomerization. The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes.
- active formcrystal structuremetastasis inhibitoroligomerizationPRL phosphatases
- Appears in Collections:
- Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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