PDBsum entry 1v3a

Hydrolase

PDB id

1v3a

Contents

			Protein chain

					162 a.a.

References listed in PDB file

Key reference

Title

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

Authors

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.

Ref.

FEBS Lett, 2004, 565, 181-187. [DOI no: 10.1016/j.febslet.2004.03.062]

PubMed id

15135076

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.



	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).

PROCHECK

	Headers