2b3o: Difference between revisions

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New page: left|200px<br /> <applet load="2b3o" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b3o, resolution 2.8Å" /> '''Crystal structure of...
 
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[[Image:2b3o.gif|left|200px]]<br />
<applet load="2b3o" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2b3o, resolution 2.8&Aring;" />
'''Crystal structure of human tyrosine phosphatase SHP-1'''<br />


==Overview==
==Crystal structure of human tyrosine phosphatase SHP-1==
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.
<StructureSection load='2b3o' size='340' side='right'caption='[[2b3o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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>


==About this Structure==
==See Also==
2B3O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B3O OCA].
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12482860 12482860]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:58:00 2007''

Latest revision as of 12:15, 14 February 2024

Crystal structure of human tyrosine phosphatase SHP-1Crystal structure of human tyrosine phosphatase SHP-1

Structural highlights

2b3o 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 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Keilhack H, Muller M, Bohmer SA, Frank C, Weidner KM, Birchmeier W, Ligensa T, Berndt A, Kosmehl H, Gunther B, Muller T, Birchmeier C, Bohmer FD. Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1. J Cell Biol. 2001 Jan 22;152(2):325-34. PMID:11266449

2b3o, resolution 2.80Å

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