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1sps

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(New page: 200px<br /><applet load="1sps" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sps, resolution 2.7&Aring;" /> '''BINDING OF A HIGH AFF...)
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[[Image:1sps.gif|left|200px]]<br /><applet load="1sps" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sps, resolution 2.7&Aring;" />
 
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'''BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS'''<br />
 
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==Overview==
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==BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS==
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The crystal structure of the Src SH2 domain complexed with a high affinity, 11-residue phosphopeptide has been determined at 2.7 A resolution by X-ray, diffraction. The peptide binds in an extended conformation and makes, primary interactions with the SH2 domain at six central residues:, PQ(pY)EEI. The phosphotyrosine and the isoleucine are tightly bound by two, well-defined pockets on the protein surface, resulting in a complex that, resembles a two-pronged plug engaging a two-holed socket. The glutamate, residues are in solvent-exposed environments in the vicinity of basic side, chains of the SH2 domain, and the two N-terminal residues cap the, phosphotyrosine-binding site. The crystal structure of Src SH2 in the, absence of peptide has been determined at 2.5 A resolution, and comparison, with the structure of the high affinity complex reveals only localized and, relatively small changes.
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<StructureSection load='1sps' size='340' side='right'caption='[[1sps]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sps]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesocricetus_auratus_polyomavirus_1 Mesocricetus auratus polyomavirus 1] and [https://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SPS 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]] 2.7&#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=1sps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sps OCA], [https://pdbe.org/1sps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sps RCSB], [https://www.ebi.ac.uk/pdbsum/1sps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sps ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SRC_RSVSA SRC_RSVSA] This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro.
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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/sp/1sps_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=1sps 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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1SPS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hamster_polyomavirus Hamster polyomavirus] and [http://en.wikipedia.org/wiki/Rous_sarcoma_virus Rous sarcoma virus] with PO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SPS OCA].
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*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms., Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J, Cell. 1993 Mar 12;72(5):779-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7680960 7680960]
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[[Category: Large Structures]]
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[[Category: Hamster polyomavirus]]
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[[Category: Mesocricetus auratus polyomavirus 1]]
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[[Category: Protein complex]]
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[[Category: Rous sarcoma virus]]
[[Category: Rous sarcoma virus]]
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[[Category: Kuriyan, J.]]
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[[Category: Kuriyan J]]
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[[Category: Waksman, G.]]
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[[Category: Waksman G]]
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[[Category: PO3]]
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[[Category: transferase(phosphotransferase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:33:12 2007''
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Current revision

BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS

PDB ID 1sps

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