1XM2

Crystal structure of Human PRL-1

1XM2 の概要

• エントリーDOI: 10.2210/pdb1xm2/pdb
• 分子名称: Tyrosine Phosphatase, SULFATE ION (3 entities 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: Q93096
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 120957.54

構造登録者

Jeong, D.G.,Kim, S.J.,Kim, J.H.,Son, J.H.,Ryu, S.E. (登録日: 2004-10-01, 公開日: 2005-01-25, 最終更新日: 2024-10-16)

主引用文献

Jeong, D.G.,Kim, S.J.,Kim, J.H.,Son, J.H.,Park, M.R.,Lim, S.M.,Yoon, T.S.,Ryu, S.E.
Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms
J.Mol.Biol., 345:401-413, 2005

PubMed Abstract: The PRL phosphatases, which constitute a subfamily of the protein tyrosine phosphatases (PTPs), are implicated in oncogenic and metastatic processes. Here, we report the crystal structure of human PRL-1 determined at 2.7A resolution. The crystal structure reveals the shallow active-site pocket with highly hydrophobic character. A structural comparison with the previously determined NMR structure of PRL-3 exhibits significant differences in the active-site region. In the PRL-1 structure, a sulfate ion is bound to the active-site, providing stabilizing interactions to maintain the canonically found active conformation of PTPs, whereas the NMR structure exhibits an open conformation of the active-site. We also found that PRL-1 forms a trimer in the crystal and the trimer exists in the membrane fraction of cells, suggesting the possible biological regulation of PRL-1 activity by oligomerization. The detailed structural information on the active enzyme conformation and regulation of PRL-1 provides the structural basis for the development of potential inhibitors of PRL enzymes.

PubMed: 15571731
DOI: 10.1016/j.jmb.2004.10.061

実験手法

X-RAY DIFFRACTION (2.7 Å)