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1fpr

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(New page: 200px<br /> <applet load="1fpr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpr, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1fpr.gif|left|200px]]<br />
 
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<applet load="1fpr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fpr, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.==
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The substrate specificity of the catalytic domain of SHP-1, an important, regulator in the proliferation and development of hematopoietic cells, is, critical for understanding the physiological functions of SHP-1. Here we, report the crystal structures of the catalytic domain of SHP-1 complexed, with two peptide substrates derived from SIRPalpha, a member of the, signal-regulatory proteins. We show that the variable beta5-loop-beta6, motif confers SHP-1 substrate specificity at the P-4 and further, N-terminal subpockets. We also observe a novel residue shift at P-2, the, highly conserved subpocket in protein- tyrosine phosphatases. Our, observations provide new insight into the substrate specificity of SHP-1.
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<StructureSection load='1fpr' size='340' side='right'caption='[[1fpr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fpr]] 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=1FPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpr OCA], [https://pdbe.org/1fpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpr RCSB], [https://www.ebi.ac.uk/pdbsum/1fpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fpr ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FPR 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=1FPR OCA].
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1., Yang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW, J Biol Chem. 2000 Feb 11;275(6):4066-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10660565 10660565]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cheng Z]]
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[[Category: Cheng, Z.]]
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[[Category: Niu Z]]
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[[Category: Niu, Z.]]
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[[Category: Yang J]]
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[[Category: Yang, J.]]
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[[Category: Zhao ZJ]]
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[[Category: Zhao, Z.J.]]
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[[Category: Zhou GW]]
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[[Category: Zhou, G.W.]]
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[[Category: protein tyrosine phosphatase]]
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[[Category: residue shift]]
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[[Category: substrate specificity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:56:01 2007''
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Current revision

CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.

PDB ID 1fpr

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