Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates

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Title
Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates
Author(s)
Keum Ran Yu; Y J Kim; S K Jung; Bonsu Ku; H Park; S Y Cho; Hye-youn Jung; S J Chung; Kwang-Hee BaeSang Chul LeeBo Yeon Kim; R L Erikson; S E Ryu; Seung Jun Kim
Bibliographic Citation
Acta Crystallographica Section D-Biological Crystallography, vol. 69, no. 8, pp. 1522-1529
Publication Year
2013
Abstract
Unlike other classical protein tyrosine phosphatases (PTPs), PTPRQ (PTP receptor type Q) has dephosphorylating activity towards phosphatidylinositide (PI) substrates. Here, the structure of the catalytic domain of PTPRQ was solved at 1.56 A resolution. Overall, PTPRQ adopts a tertiary fold typical of other classical PTPs. However, the disordered M6 loop of PTPRQ surrounding the catalytic core and the concomitant absence of interactions of this loop with residues in the PTP loop results in a flat active-site pocket. On the basis of structural and biochemical analyses, it is proposed that this structural feature might facilitate the accommodation of large substrates, making it suitable for the dephosphorylation of PI substrates. Moreover, subsequent kinetic experiments showed that PTPRQ has a strong preferences for PI(3,4,5)P3 over other PI substrates, suggesting that its regulation of cell survival and proliferation reflects downregulation of Akt signalling.
Keyword
protein tyrosine phosphatasesPTP receptor type Q
ISSN
0907-4449
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S0907444913010457
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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