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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms.

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 2.7A 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.[1]

References

  1. Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. Jeong, D.G., Kim, S.J., Kim, J.H., Son, J.H., Park, M.R., Lim, S.M., Yoon, T.S., Ryu, S.E. J. Mol. Biol. (2005) [Pubmed]
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