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

Kyoung Ah Kim; Jin Sue Song; Jun Goo Jee; Mee Rie Sheen; Chulhyun Lee; Tae Gyu Lee; Seonggu Ro; Joong Myung Cho; Weontae Lee; Toshio Yamazaki; Young Ho Jeon; Chaejoon Cheong

doi:10.1016/j.febslet.2004.03.062

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

Kyoung Ah Kim, Jin Sue Song, Jun Goo Jee, Mee Rie Sheen, Chulhyun Lee, Tae Gyu Lee, Seonggu Ro, Joong Myung Cho, Weontae Lee, Toshio Yamazaki, Young Ho Jeon, Chaejoon Cheong

Research output: Contribution to journal › Article › peer-review

60 Scopus citations

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.

Original language	English
Pages (from-to)	181-187
Number of pages	7
Journal	FEBS Letters
Volume	565
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.03.062
State	Published - 7 May 2004

Keywords

DSP, dual-specificity phosphatase
DSS, 4,4-dimethyl 4-silapentane sodium sulfonate
DTT, dithiothreitol
Metastasis
NMR
NMR, nuclear magnetic resonance
Phosphatase
PRL-3
PTP, protein tyrosine phosphatase
Structure

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.febslet.2004.03.062

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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.",

keywords = "DSP, dual-specificity phosphatase, DSS, 4,4-dimethyl 4-silapentane sodium sulfonate, DTT, dithiothreitol, Metastasis, NMR, NMR, nuclear magnetic resonance, Phosphatase, PRL-3, PTP, protein tyrosine phosphatase, Structure",

author = "Kim, {Kyoung Ah} and Song, {Jin Sue} and Jee, {Jun Goo} and Sheen, {Mee Rie} and Chulhyun Lee and Lee, {Tae Gyu} and Seonggu Ro and Cho, {Joong Myung} and Weontae Lee and Toshio Yamazaki and Jeon, {Young Ho} and Chaejoon Cheong",

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doi = "10.1016/j.febslet.2004.03.062",

language = "English",

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T1 - Structure of human PRL-3, the phosphatase associated with cancer metastasis

AU - Kim, Kyoung Ah

AU - Song, Jin Sue

AU - Jee, Jun Goo

AU - Sheen, Mee Rie

AU - Lee, Chulhyun

AU - Lee, Tae Gyu

AU - Ro, Seonggu

AU - Cho, Joong Myung

AU - Lee, Weontae

AU - Yamazaki, Toshio

AU - Jeon, Young Ho

AU - Cheong, Chaejoon

PY - 2004/5/7

Y1 - 2004/5/7

N2 - 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.

AB - 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.

KW - DSP, dual-specificity phosphatase

KW - DSS, 4,4-dimethyl 4-silapentane sodium sulfonate

KW - DTT, dithiothreitol

KW - Metastasis

KW - NMR

KW - NMR, nuclear magnetic resonance

KW - Phosphatase

KW - PRL-3

KW - PTP, protein tyrosine phosphatase

KW - Structure

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DO - 10.1016/j.febslet.2004.03.062

M3 - Article

C2 - 15135076

AN - SCOPUS:2342658395

SN - 0014-5793

VL - 565

SP - 181

EP - 187

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

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

Abstract

Keywords

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