Structure of human PRL-3, the phosphatase associated with cancer metastasis

Kyoung Ah Kim, Jin Sue Song, Jun Goo Jee, Mee Rie Sheen, Chulhyun Lee, Tae Gyu Lee, Seonggu Ro, Joong Myung Cho, Weontae Lee, Toshio Yamazaki, Young Ho Jeon, Chaejoon Cheong

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Abstract

PRL-3, a novel class protein of prenylated tyrosine phosphatase, is important in cancer metastasis. Due to its high levels of expression in metastatic tumors, PRL-3 may constitute a useful marker for metastasis and might be a new therapeutic target. Here, we present the solution structure of the phosphatase domain of a human PRL-3 (residues 1-162) in phosphate-free state. The nuclear magnetic resonance (NMR) structure of PRL-3 is similar to that of other known phosphatases with minor differences in the secondary structure. But the conformation and flexibility of the loops comprising the active site differ significantly. When phosphate ions or sodium orthovanadate, which is a known inhibitor, are added to the apo PRL-3, the NMR signals from the residues in the active site appeared and could be assigned, indicating that the conformation of the residues has been stabilized.

Original languageEnglish
Pages (from-to)181-187
Number of pages7
JournalFEBS Letters
Volume565
Issue number1-3
DOIs
Publication statusPublished - 2004 May 7

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Kim, K. A., Song, J. S., Jee, J. G., Sheen, M. R., Lee, C., Lee, T. G., Ro, S., Cho, J. M., Lee, W., Yamazaki, T., Jeon, Y. H., & Cheong, C. (2004). Structure of human PRL-3, the phosphatase associated with cancer metastasis. FEBS Letters, 565(1-3), 181-187. https://doi.org/10.1016/j.febslet.2004.03.062