4IKC

Crystal Structure of catalytic domain of PTPRQ

Summary for 4IKC

• Entry DOI: 10.2210/pdb4ikc/pdb
• Descriptor: Phosphotidylinositol phosphatase PTPRQ, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: phosphatase, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: Q9UMZ3
• Total number of polymer chains: 1
• Total formula weight: 32473.52

Authors

Yu, K.R.,Ryu, S.E.,Kim, S.J. (deposition date: 2012-12-26, release date: 2013-07-31, Last modification date: 2023-11-08)

Primary citation

Yu, K.R.,Kim, Y.J.,Jung, S.K.,Ku, B.,Park, H.,Cho, S.Y.,Jung, H.,Chung, S.J.,Bae, K.H.,Lee, S.C.,Kim, B.Y.,Erikson, R.L.,Ryu, S.E.,Kim, S.J.
Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates
Acta Crystallogr.,Sect.D, 69:1522-1529, 2013

PubMed 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 Å 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.

PubMed: 23897475
DOI: 10.1107/S0907444913010457

Experimental method

X-RAY DIFFRACTION (1.56 Å)