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Title 

Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates

Authors 

Keum Ran YuY J KimS K JungBonsu KuH ParkS Y ChoHye-youn JungS J ChungKwang-Hee BaeSang Chul LeeBo Yeon KimR L EriksonS E RyuSeung Jun Kim

Publisher 

International Union of Crystallography

Issue Date 

2013

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 69, no. 8, pp. 1522-1529

Keywords 

protein tyrosine phosphatasesPTP receptor type Q

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 ? 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.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 69(8): 1522-1529

ISSN 

0907-4449

Link 

http://dx.doi.org/10.1107/S0907444913010457

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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