1V3A
Structure of human PRL-3, the phosphatase associated with cancer metastasis
Summary for 1V3A
| Entry DOI | 10.2210/pdb1v3a/pdb |
| Descriptor | protein tyrosine phosphatase type IVA (1 entity in total) |
| Functional Keywords | hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane: O75365 |
| Total number of polymer chains | 1 |
| Total formula weight | 19566.90 |
| Authors | Jeon, Y.H.,Cheong, C. (deposition date: 2003-10-30, release date: 2004-10-30, Last modification date: 2023-12-27) |
| Primary citation | Kim, K.A.,Song, J.S.,Jee, J.,Sheen, M.R.,Lee, C.,Lee, T.G.,Ro, S.,Cho, J.M.,Lee, W.,Yamazaki, T.,Jeon, Y.H.,Cheong, C. Structure of human PRL-3, the phosphatase associated with cancer metastasis Febs Lett., 565:181-187, 2004 Cited by PubMed 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. PubMed: 15135076DOI: 10.1016/j.febslet.2004.03.062 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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