title: Structure of human PRL-3, the phosphatase associated with cancer metastasis.
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.
authors.affiliation: Magnetic Resonance Team, Korea Basic Science Institute, Daejeon 305-333, Republic of Korea.
authors.forename: Kyoung-Ah
authors.initials: KA
authors.lastname: Kim
authors.forename: Jin-Sue
authors.initials: JS
authors.lastname: Song
authors.forename: JunGoo
authors.initials: J
authors.lastname: Jee
authors.forename: Mee Rie
authors.initials: MR
authors.lastname: Sheen
authors.forename: Chulhyun
authors.initials: C
authors.lastname: Lee
authors.forename: Tae Gyu
authors.initials: TG
authors.lastname: Lee
authors.forename: Seonggu
authors.initials: S
authors.lastname: Ro
authors.forename: Joong Myung
authors.initials: JM
authors.lastname: Cho
authors.forename: Weontae
authors.initials: W
authors.lastname: Lee
authors.forename: Toshio
authors.initials: T
authors.lastname: Yamazaki
authors.forename: Young Ho
authors.initials: YH
authors.lastname: Jeon
authors.forename: Chaejoon
authors.initials: C
authors.lastname: Cheong
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D017874:Immediate-Early Proteins / Q000737:chemistry*; D007477:Ions; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009362:Neoplasm Metastasis; D009363:Neoplasm Proteins; D009369:Neoplasms / Q000201:enzymology* / Q000473:pathology*; D010710:Phosphates / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014443:Tyrosine / Q000737:chemistry; D014638:Vanadates / Q000737:chemistry / Q000494:pharmacology
chemical_list: D004791:Enzyme Inhibitors; D017874:Immediate-Early Proteins; D007477:Ions; D008024:Ligands; D009363:Neoplasm Proteins; D010710:Phosphates; D014638:Vanadates; D014443:Tyrosine; C484730:PTP4A3 protein, human; D017027:Protein Tyrosine Phosphatases