1V3A

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

1V3A の概要

• エントリーDOI: 10.2210/pdb1v3a/pdb
• 分子名称: protein tyrosine phosphatase type IVA (1 entity in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane: O75365
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19566.90

構造登録者

Jeon, Y.H.,Cheong, C. (登録日: 2003-10-30, 公開日: 2004-10-30, 最終更新日: 2023-12-27)

主引用文献

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

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: 15135076
DOI: 10.1016/j.febslet.2004.03.062

実験手法

SOLUTION NMR