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3mbk

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Revision as of 07:55, 25 December 2014

The 1.35 A Structure of the Phosphatase Domain of the Suppressor of T Cell Receptor Signalling Protein in Complex with Sulphate

Structural highlights

3mbk is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2h0q
Gene:	Ubash3b (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[UBS3B_MOUSE] Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The suppressor of T-cell signaling (Sts) proteins are multidomain proteins that negatively regulate the signaling of membrane-bound receptors, including the T-cell receptor (TCR) and the epidermal growth-factor receptor (EGFR). They contain at their C-terminus a 2H-phosphatase homology (PGM) domain that is responsible for their protein tyrosine phosphatase activity. Here, the crystal structure of the phosphatase domain of Sts-1, Sts-1(PGM), was determined at pH 4.6. The asymmetric unit contains two independent molecules and each active site is occupied by a sulfate ion. Each sulfate is located at the phosphate-binding site and makes similar interactions with the catalytic residues. The structure suggests an explanation for the lower Michaelis-Menten constants at acidic pH.

The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate.,Jakoncic J, Sondgeroth B, Carpino N, Nassar N Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt, 6):643-7. Epub 2010 May 25. PMID:20516590^[5]

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

References

↑ Carpino N, Turner S, Mekala D, Takahashi Y, Zang H, Geiger TL, Doherty P, Ihle JN. Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2. Immunity. 2004 Jan;20(1):37-46. PMID:14738763
↑ Carpino N, Chen Y, Nassar N, Oh HW. The Sts proteins target tyrosine phosphorylated, ubiquitinated proteins within TCR signaling pathways. Mol Immunol. 2009 Oct;46(16):3224-31. Epub 2009 Sep 5. PMID:19733910 doi:S0161-5890(09)00679-8
↑ Thomas DH, Getz TM, Newman TN, Dangelmaier CA, Carpino N, Kunapuli SP, Tsygankov AY, Daniel JL. A novel histidine tyrosine phosphatase, TULA-2, associates with Syk and negatively regulates GPVI signaling in platelets. Blood. 2010 Oct 7;116(14):2570-8. doi: 10.1182/blood-2010-02-268136. Epub 2010, Jun 28. PMID:20585042 doi:10.1182/blood-2010-02-268136
↑ Mikhailik A, Ford B, Keller J, Chen Y, Nassar N, Carpino N. A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling. Mol Cell. 2007 Aug 3;27(3):486-97. PMID:17679096 doi:10.1016/j.molcel.2007.06.015
↑ Jakoncic J, Sondgeroth B, Carpino N, Nassar N. The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt, 6):643-7. Epub 2010 May 25. PMID:20516590 doi:10.1107/S1744309110014259

1 Structural highlights
2 Function
3 Evolutionary Conservation
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/3mbk"

@@ Line 8: / Line 8: @@
 <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=3mbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mbk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mbk RCSB], [http://www.ebi.ac.uk/pdbsum/3mbk PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/UBS3B_MOUSE UBS3B_MOUSE]] Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.<ref>PMID:14738763</ref> <ref>PMID:19733910</ref> <ref>PMID:20585042</ref> <ref>PMID:17679096</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3mbk

From Proteopedia

Revision as of 07:55, 25 December 2014

The 1.35 A Structure of the Phosphatase Domain of the Suppressor of T Cell Receptor Signalling Protein in Complex with Sulphate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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