1XM2

Crystal structure of Human PRL-1

Summary for 1XM2

• Entry DOI: 10.2210/pdb1xm2/pdb
• Descriptor: Tyrosine Phosphatase, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane: Q93096
• Total number of polymer chains: 6
• Total formula weight: 120957.54

Authors

Jeong, D.G.,Kim, S.J.,Kim, J.H.,Son, J.H.,Ryu, S.E. (deposition date: 2004-10-01, release date: 2005-01-25, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)