2y96

From Proteopedia

(Difference between revisions)

Current revision

Structure of human dual-specificity phosphatase 27

Structural highlights

2y96 is a 2 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 2.38Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DUS29_HUMAN Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (PubMed:17498703). Involved in the modulation of intracellular signaling cascades. In skeletal muscle regulates systemic glucose homeostasis by activating, AMPK, an energy sensor protein kinase (By similarity). Affects MAP kinase signaling though modulation of the MAPK1/2 cascade in skeletal muscle promoting muscle cell differentiation, development and atrophy (By similarity).[UniProtKB:Q8BK84]^[1]

Publication Abstract from PubMed

There are over 100 genes in the human genome that encode protein tyrosine phosphatases (PTPs) and approximately 60 of these are classified as dual-specificity phosphatases (DUSPs). Although many dual-specificity phosphatases are still not well characterized, novel functions have been discovered for some of them that have led to new insights into a variety of biological processes and the molecular basis for certain diseases. Indeed, as the functions of DUSPs continue to be elucidated, a growing number of them are emerging as potential therapeutic targets for diseases such as cancer, diabetes and inflammatory disorders. Here, the overexpression, purification and structure determination of DUSP27 at 2.38 A resolution are presented.

Structure of human dual-specificity phosphatase 27 at 2.38 A resolution.,Lountos GT, Tropea JE, Waugh DS Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):471-9. Epub 2011, Apr 16. PMID:21543850^[2]

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

References

↑ Friedberg I, Nika K, Tautz L, Saito K, Cerignoli F, Friedberg I, Godzik A, Mustelin T. Identification and characterization of DUSP27, a novel dual-specific protein phosphatase. FEBS Lett. 2007 May 29;581(13):2527-33. PMID:17498703 doi:10.1016/j.febslet.2007.04.059
↑ Lountos GT, Tropea JE, Waugh DS. Structure of human dual-specificity phosphatase 27 at 2.38 A resolution. Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):471-9. Epub 2011, Apr 16. PMID:21543850 doi:10.1107/S090744491100970X

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/2y96"

Categories: Homo sapiens | Large Structures | Lountos GT | Tropea JE | Waugh DS

@@ Line 3: / Line 3: @@
 <StructureSection load='2y96' size='340' side='right'caption='[[2y96]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y96]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y96 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y96]] is a 2 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=2Y96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y96 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.38&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2y96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y96 OCA], [https://pdbe.org/2y96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y96 RCSB], [https://www.ebi.ac.uk/pdbsum/2y96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y96 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/DUS29_HUMAN DUS29_HUMAN] Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (PubMed:17498703). Involved in the modulation of intracellular signaling cascades. In skeletal muscle regulates systemic glucose homeostasis by activating, AMPK, an energy sensor protein kinase (By similarity). Affects MAP kinase signaling though modulation of the MAPK1/2 cascade in skeletal muscle promoting muscle cell differentiation, development and atrophy (By similarity).[UniProtKB:Q8BK84]<ref>PMID:17498703</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Lountos, G T]]
+[[Category: Lountos GT]]
-[[Category: Tropea, J E]]
+[[Category: Tropea JE]]
-[[Category: Waugh, D S]]
+[[Category: Waugh DS]]
-[[Category: Hydrolase]]

2y96

From Proteopedia

Current revision

Structure of human dual-specificity phosphatase 27

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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