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Title 

Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms

Authors 

Dae Gwin JeongSeung-Jun KimJ H KimJeong Hee SonMi Rim ParkSang Myoun LimTae-Sung YoonSeong Eon Ryu

Publisher 

Elsevier

Issue Date 

2005

Citation 

Journal of Molecular Biology, vol. 345, no. 2, pp. 401-413

Keywords 

active formcrystal structuremetastasis inhibitoroligomerizationPRL phosphatasesisoenzymephosphatase of regenerating liver 1phosphatase of regenerating liver 3protein tyrosine phosphatase

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 2.7 ? 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.

ISSN 

0022-2836

Link 

http://dx.doi.org/10.1016/j.jmb.2004.10.061

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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