This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2b3o

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:27, 16 May 2018

Crystal structure of human tyrosine phosphatase SHP-1

Structural highlights

2b3o is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1gwz, 1fpr
Gene:	PTPN6, HCP, PTP1C (HUMAN)
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
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.

Publication Abstract from PubMed

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.

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:12482860^[2]

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

References

↑ 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
↑ Yang J, Liu L, He D, Song X, Liang X, Zhao ZJ, Zhou GW. Crystal structure of human protein-tyrosine phosphatase SHP-1. J Biol Chem. 2003 Feb 21;278(8):6516-20. Epub 2002 Dec 13. PMID:12482860 doi:10.1074/jbc.M210430200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b3o"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human tyrosine phosphatase SHP-1==
 <StructureSection load='2b3o' size='340' side='right' caption='[[2b3o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPN6, HCP, PTP1C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='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=2b3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3o OCA], [http://pdbe.org/2b3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b3o RCSB], [http://www.ebi.ac.uk/pdbsum/2b3o PDBsum]</span></td></tr>
+<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=2b3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3o OCA], [http://pdbe.org/2b3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b3o RCSB], [http://www.ebi.ac.uk/pdbsum/2b3o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b3o ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/2b3o_consurf.spt"</scriptWhenChecked>
+    <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>

2b3o

From Proteopedia

Revision as of 06:27, 16 May 2018

Crystal structure of human tyrosine phosphatase SHP-1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox