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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57 Citations (Scopus)


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
Issue number1-3
Publication statusPublished - 2004 May 7

Bibliographical note

Funding Information:
This work was supported by the Consortium Program of the SMBA and by the National Research Laboratory Program of the MOST, the Republic of Korea.

All Science Journal Classification (ASJC) codes

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


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