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1qwf

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[[Image:1qwf.jpg|left|200px]]
 
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{{Structure
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==C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12==
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|PDB= 1qwf |SIZE=350|CAPTION= <scene name='initialview01'>1qwf</scene>
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<StructureSection load='1qwf' size='340' side='right'caption='[[1qwf]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= CHICKEN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11876 Avian sarcoma virus])
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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=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>
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}}
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</table>
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== Function ==
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[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.
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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/qw/1qwf_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=1qwf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12'''
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1qwf" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1QWF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWF OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8618911 8618911]
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[[Category: Avian sarcoma virus]]
[[Category: Avian sarcoma virus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Transferase]]
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[[Category: Chiyoshi K]]
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[[Category: Chiyoshi, K.]]
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[[Category: Feng S]]
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[[Category: Feng, S.]]
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[[Category: Rickles RJ]]
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[[Category: Rickles, R J.]]
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[[Category: Schreiber SL]]
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[[Category: Schreiber, S L.]]
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[[Category: class i ligand complex]]
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[[Category: src sh3 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:36 2008''
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Current revision

C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12

PDB ID 1qwf

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