2b3o: Difference between revisions

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-[[Image:2b3o.gif|left|200px]]
- {{Structure
+==Crystal structure of human tyrosine phosphatase SHP-1==
-|PDB= 2b3o |SIZE=350|CAPTION= <scene name='initialview01'>2b3o</scene>, resolution 2.8&Aring;
+<StructureSection load='2b3o' size='340' side='right'caption='[[2b3o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[2b3o]] 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=2B3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B3O FirstGlance]. <br>
-|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-|GENE= PTPN6, HCP, PTP1C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3o OCA], [https://pdbe.org/2b3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b3o RCSB], [https://www.ebi.ac.uk/pdbsum/2b3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b3o ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=[[1gwz|1GWZ]], [[1fpr|1FPR]]
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3o OCA], [http://www.ebi.ac.uk/pdbsum/2b3o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b3o RCSB]</span>
+[https://www.uniprot.org/uniprot/PTN6_HUMAN PTN6_HUMAN] Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis.<ref>PMID:11266449</ref>
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/2b3o_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b3o ConSurf].
+<div style="clear:both"></div>
-'''Crystal structure of human tyrosine phosphatase SHP-1'''
+==See Also==
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
+== References ==
-==Overview==
+<references/>
-SHP-1 is a cytosolic protein-tyrosine phosphatase that behaves as a negative regulator in eukaryotic cellular signaling pathways. To understand its regulatory mechanism, we have determined the crystal structure of the C-terminal truncated human SHP-1 in the inactive conformation at 2.8-A resolution and refined the structure to a crystallographic R-factor of 24.0%. The three-dimensional structure shows that the ligand-free SHP-1 has an auto-inhibited conformation. Its N-SH2 domain blocks the catalytic domain and keeps the enzyme in the inactive conformation, which supports that the phosphatase activity of SHP-1 is primarily regulated by the N-SH2 domain. In addition, the C-SH2 domain of SHP-1 has a different orientation from and is more flexible than that of SHP-2, which enables us to propose an enzymatic activation mechanism in which the C-SH2 domains of SHPs could be involved in searching for phosphotyrosine activators.
+__TOC__
+</StructureSection>
-==About this Structure==
-B3O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3O OCA].
-==Reference==
-Crystal structure of human protein-tyrosine phosphatase SHP-1., Yang J, Liu L, He D, Song X, Liang X, Zhao ZJ, Zhou GW, J Biol Chem. 2003 Feb 21;278(8):6516-20. Epub 2002 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12482860 12482860]
 [[Category: Homo sapiens]]
-[[Category: Protein-tyrosine-phosphatase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: He D]]
-[[Category: He, D.]]
+[[Category: Liang X]]
-[[Category: Liang, X.]]
+[[Category: Liu L]]
-[[Category: Liu, L.]]
+[[Category: Song X]]
-[[Category: Song, X.]]
+[[Category: Yang J]]
-[[Category: Yang, J.]]
+[[Category: Zhao ZJ]]
-[[Category: Zhao, Z J.]]
+[[Category: Zhou GW]]
-[[Category: Zhou, G W.]]
-[[Category: protein tyrosine phosphatase]]
-[[Category: shp-1]]
-[[Category: signaling]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:00:59 2008''