2b3o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:15, 14 February 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2b3o.gif|left|200px]]
 
-
<!--
+
==Crystal structure of human tyrosine phosphatase SHP-1==
-
The line below this paragraph, containing "STRUCTURE_2b3o", creates the "Structure Box" on the page.
+
<StructureSection load='2b3o' size='340' side='right'caption='[[2b3o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</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>
-
{{STRUCTURE_2b3o| PDB=2b3o | SCENE= }}
+
</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>
-
'''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==
+
-
2B3O 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: 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 Sat May 3 19:48:44 2008''
+

Current revision

Crystal structure of human tyrosine phosphatase SHP-1

PDB ID 2b3o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools