1v3a

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

Structural highlights

1v3a is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TP4A3_HUMAN Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structure of human PRL-3, the phosphatase associated with cancer metastasis.,Kim KA, Song JS, Jee J, Sheen MR, Lee C, Lee TG, Ro S, Cho JM, Lee W, Yamazaki T, Jeon YH, Cheong C FEBS Lett. 2004 May 7;565(1-3):181-7. PMID:15135076[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
9 reviews cite this structure
PRL PTPs: mediators and markers of cancer progression.
Bessette et al. (2008)
8 more
27 other articles
No citations found

See Also

References

  1. ↑ Matter WF, Estridge T, Zhang C, Belagaje R, Stancato L, Dixon J, Johnson B, Bloem L, Pickard T, Donaghue M, Acton S, Jeyaseelan R, Kadambi V, Vlahos CJ. Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling. Biochem Biophys Res Commun. 2001 May 25;283(5):1061-8. PMID:11355880 doi:http://dx.doi.org/10.1006/bbrc.2001.4881
  2. ↑ Zeng Q, Dong JM, Guo K, Li J, Tan HX, Koh V, Pallen CJ, Manser E, Hong W. PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. Cancer Res. 2003 Jun 1;63(11):2716-22. PMID:12782572
  3. ↑ Kim KA, Song JS, Jee J, Sheen MR, Lee C, Lee TG, Ro S, Cho JM, Lee W, Yamazaki T, Jeon YH, Cheong C. Structure of human PRL-3, the phosphatase associated with cancer metastasis. FEBS Lett. 2004 May 7;565(1-3):181-7. PMID:15135076 doi:10.1016/j.febslet.2004.03.062

Contents


PDB ID 1v3a

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