Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates
- Title
- Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates
- Author
- 류성언
- Keywords
- PTP receptor type Q; protein tyrosine phosphatases.
- Issue Date
- 2013-08
- Publisher
- WILEY-BLACKWELL
- Citation
- Acta crystallographica. Section D, Biological crystallography, Aug 2013, 69(8), P.1522 - 1529
- 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 angstrom 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)P-3 over other PI substrates, suggesting that its regulation of cell survival and proliferation reflects downregulation of Akt signalling.
- URI
- http://scripts.iucr.org/cgi-bin/paper?S0907444913010457http://hdl.handle.net/20.500.11754/53997
- ISSN
- 0907-4449; 1399-0047
- DOI
- 10.1107/S0907444913010457
- Appears in Collections:
- COLLEGE OF ENGINEERING[S](공과대학) > BIOENGINEERING(생명공학과) > Articles
- Files in This Item:
There are no files associated with this item.
- Export
- RIS (EndNote)
- XLS (Excel)
- XML