PDBsum entry 1v3a

Hydrolase

PDB id: 1v3a

Contents

Protein chain

162 a.a. *

* Residue conservation analysis

PDB id:

1v3a

Name:

Hydrolase

Title:

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

Structure:

Protein tyrosine phosphatase type iva. Chain: a. Synonym: phosphatase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

Y.H.Jeon,C.Cheong

Key ref:

K.A.Kim et al. (2004). Structure of human PRL-3, the phosphatase associated with cancer metastasis. FEBS Lett, 565, 181-187. PubMed id: 15135076 DOI: 10.1016/j.febslet.2004.03.062

Date:

30-Oct-03 Release date: 30-Oct-04

Protein chain

O75365  (TP4A3_HUMAN) -  Protein tyrosine phosphatase type IVA 3 from Homo sapiens

Seq: 173 a.a.

Struc: 162 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - protein-tyrosine-phosphatase.
• Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

DOI no: 10.1016/j.febslet.2004.03.062

FEBS Lett 565:181-187 (2004)

PubMed id: 15135076

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

K.A.Kim, J.S.Song, J.Jee, M.R.Sheen, C.Lee, T.G.Lee, S.Ro, J.M.Cho, W.Lee, T.Yamazaki, Y.H.Jeon, C.Cheong.

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.

Selected figure(s)

Figure 3.
Fig. 3. A comparison of three structures. (A) PRL-3, (B) PAC-1, and (C) PTEN. Residues Cys104 and Arg110 of PRL-3 are marked by filled circles. Asp72 in the general acid loop of PRL-3 and the corresponding residues in PAC-1 and PTEN are shown using a ball-and-stick model.

Figure 4.
Fig. 4. Overlapping ^1H–^15N HSQC spectra of PRL-3 obtained in the presence and absence of ligand ions. The peaks representing the free form of the protein are shown in black. (A) 0.7 mM PRL-3 with 2 mM sodium orthovanadate (brown), (B) 0.7 mM PRL-3 with 20 mM phosphate (purple). The red circled peaks are the backbone amide protons that appeared in the active site (phosphate loop).

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2004, 565, 181-187) copyright 2004.

Figures were selected by an automated process.