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1qwf
From Proteopedia
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| - | [[Image:1qwf.jpg|left|200px]]<br /><applet load="1qwf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1qwf" /> | ||
| - | '''C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12'''<br /> | ||
| - | == | + | ==C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12== |
| + | <StructureSection load='1qwf' size='340' side='right'caption='[[1qwf]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1qwf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QWF FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1qwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwf OCA], [https://pdbe.org/1qwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwf RCSB], [https://www.ebi.ac.uk/pdbsum/1qwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SRC_AVISR SRC_AVISR] 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. | ||
| + | == 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/qw/1qwf_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=1qwf ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligant residues flanking the proline-rich core. The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity. | Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligant residues flanking the proline-rich core. The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity. | ||
| - | + | Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands.,Feng S, Kasahara C, Rickles RJ, Schreiber SL Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):12408-15. PMID:8618911<ref>PMID:8618911</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1qwf" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Avian sarcoma virus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chiyoshi K]] | ||
| + | [[Category: Feng S]] | ||
| + | [[Category: Rickles RJ]] | ||
| + | [[Category: Schreiber SL]] | ||
Current revision
C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12
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