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4ikc

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Revision as of 07:22, 5 August 2016

Crystal Structure of catalytic domain of PTPRQ

Structural highlights

4ikc is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	PTPRQ (HUMAN)
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[PTPRQ_HUMAN] Autosomal recessive nonsyndromic sensorineural deafness type DFNB. The disease is caused by mutations affecting the gene represented in this entry.

Function

[PTPRQ_HUMAN] Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells.^[1]

Publication Abstract from PubMed

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.

Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates.,Yu KR, Kim YJ, Jung SK, Ku B, Park H, Cho SY, Jung H, Chung SJ, Bae KH, Lee SC, Kim BY, Erikson RL, Ryu SE, Kim SJ Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1522-9. doi:, 10.1107/S0907444913010457. Epub 2013 Jul 19. PMID:23897475^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jung H, Kim WK, Kim do H, Cho YS, Kim SJ, Park SG, Park BC, Lim HM, Bae KH, Lee SC. Involvement of PTP-RQ in differentiation during adipogenesis of human mesenchymal stem cells. Biochem Biophys Res Commun. 2009 May 29;383(2):252-7. doi:, 10.1016/j.bbrc.2009.04.001. Epub 2009 Apr 5. PMID:19351528 doi:10.1016/j.bbrc.2009.04.001
↑ Yu KR, Kim YJ, Jung SK, Ku B, Park H, Cho SY, Jung H, Chung SJ, Bae KH, Lee SC, Kim BY, Erikson RL, Ryu SE, Kim SJ. Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1522-9. doi:, 10.1107/S0907444913010457. Epub 2013 Jul 19. PMID:23897475 doi:http://dx.doi.org/10.1107/S0907444913010457

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ikc"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of catalytic domain of PTPRQ==
 <StructureSection load='4ikc' size='340' side='right' caption='[[4ikc]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ikc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ikc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ikc RCSB], [http://www.ebi.ac.uk/pdbsum/4ikc PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ikc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ikc OCA], [http://pdbe.org/4ikc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ikc RCSB], [http://www.ebi.ac.uk/pdbsum/4ikc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ikc ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 20: / Line 21: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ikc" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ikc

From Proteopedia

Revision as of 07:22, 5 August 2016

Crystal Structure of catalytic domain of PTPRQ

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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