6suc

From Proteopedia

(Difference between revisions)

Revision as of 12:48, 24 January 2024

Human PTPRU D1 domain, oxidised form

Structural highlights

6suc is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.97Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTPRU_HUMAN Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The receptor-linked protein tyrosine phosphatases (RPTPs) are key regulators of cell-cell communication through the control of cellular phosphotyrosine levels. Most human RPTPs possess an extracellular receptor domain and tandem intracellular phosphatase domains: comprising an active membrane proximal (D1) domain and an inactive distal (D2) pseudophosphatase domain. Here we demonstrate that PTPRU is unique amongst the RPTPs in possessing two pseudophosphatase domains. The PTPRU-D1 displays no detectable catalytic activity against a range of phosphorylated substrates and we show that this is due to multiple structural rearrangements that destabilise the active site pocket and block the catalytic cysteine. Upon oxidation, this cysteine forms an intramolecular disulphide bond with a vicinal "backdoor" cysteine, a process thought to reversibly inactivate related phosphatases. Importantly, despite the absence of catalytic activity, PTPRU binds substrates of related phosphatases strongly suggesting that this pseudophosphatase functions in tyrosine phosphorylation by competing with active phosphatases for the binding of substrates.

The receptor PTPRU is a redox sensitive pseudophosphatase.,Hay IM, Fearnley GW, Rios P, Kohn M, Sharpe HJ, Deane JE Nat Commun. 2020 Jun 26;11(1):3219. doi: 10.1038/s41467-020-17076-w. PMID:32591542^[4]

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

References

↑ Taniguchi Y, London R, Schinkmann K, Jiang S, Avraham H. The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and Is associated with the c-Kit receptor. Blood. 1999 Jul 15;94(2):539-49. PMID:10397721
↑ Yan HX, He YQ, Dong H, Zhang P, Zeng JZ, Cao HF, Wu MC, Wang HY. Physical and functional interaction between receptor-like protein tyrosine phosphatase PCP-2 and beta-catenin. Biochemistry. 2002 Dec 31;41(52):15854-60. PMID:12501215 doi:10.1021/bi026095u
↑ Yan HX, Yang W, Zhang R, Chen L, Tang L, Zhai B, Liu SQ, Cao HF, Man XB, Wu HP, Wu MC, Wang HY. Protein-tyrosine phosphatase PCP-2 inhibits beta-catenin signaling and increases E-cadherin-dependent cell adhesion. J Biol Chem. 2006 Jun 2;281(22):15423-33. PMID:16574648 doi:10.1074/jbc.M602607200
↑ Hay IM, Fearnley GW, Rios P, Köhn M, Sharpe HJ, Deane JE. The receptor PTPRU is a redox sensitive pseudophosphatase. Nat Commun. 2020 Jun 26;11(1):3219. PMID:32591542 doi:10.1038/s41467-020-17076-w

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6suc"

@@ Line 1: / Line 1: @@
 ==Human PTPRU D1 domain, oxidised form==
-<StructureSection load='6suc' size='340' side='right'caption='[[6suc]]' scene=''>
+<StructureSection load='6suc' size='340' side='right'caption='[[6suc]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SUC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SUC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6suc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SUC FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6suc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6suc OCA], [http://pdbe.org/6suc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6suc RCSB], [http://www.ebi.ac.uk/pdbsum/6suc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6suc ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6suc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6suc OCA], [https://pdbe.org/6suc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6suc RCSB], [https://www.ebi.ac.uk/pdbsum/6suc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6suc ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PTPRU_HUMAN PTPRU_HUMAN] Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis.<ref>PMID:10397721</ref> <ref>PMID:12501215</ref> <ref>PMID:16574648</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The receptor-linked protein tyrosine phosphatases (RPTPs) are key regulators of cell-cell communication through the control of cellular phosphotyrosine levels. Most human RPTPs possess an extracellular receptor domain and tandem intracellular phosphatase domains: comprising an active membrane proximal (D1) domain and an inactive distal (D2) pseudophosphatase domain. Here we demonstrate that PTPRU is unique amongst the RPTPs in possessing two pseudophosphatase domains. The PTPRU-D1 displays no detectable catalytic activity against a range of phosphorylated substrates and we show that this is due to multiple structural rearrangements that destabilise the active site pocket and block the catalytic cysteine. Upon oxidation, this cysteine forms an intramolecular disulphide bond with a vicinal "backdoor" cysteine, a process thought to reversibly inactivate related phosphatases. Importantly, despite the absence of catalytic activity, PTPRU binds substrates of related phosphatases strongly suggesting that this pseudophosphatase functions in tyrosine phosphorylation by competing with active phosphatases for the binding of substrates.
+The receptor PTPRU is a redox sensitive pseudophosphatase.,Hay IM, Fearnley GW, Rios P, Kohn M, Sharpe HJ, Deane JE Nat Commun. 2020 Jun 26;11(1):3219. doi: 10.1038/s41467-020-17076-w. PMID:32591542<ref>PMID:32591542</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6suc" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
 [[Category: Deane JE]]

6suc

From Proteopedia

Revision as of 12:48, 24 January 2024

Human PTPRU D1 domain, oxidised form

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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