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[[Image:1qwe.jpg|left|200px]]


{{Structure
==C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND APP12==
|PDB= 1qwe |SIZE=350|CAPTION= <scene name='initialview01'>1qwe</scene>
<StructureSection load='1qwe' size='340' side='right'caption='[[1qwe]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1qwe]] 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=1QWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QWE FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE= CHICKEN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11876 Avian sarcoma virus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwe OCA], [https://pdbe.org/1qwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwe RCSB], [https://www.ebi.ac.uk/pdbsum/1qwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwe ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwe OCA], [http://www.ebi.ac.uk/pdbsum/1qwe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qwe RCSB]</span>
[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/1qwe_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=1qwe 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.


'''C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND APP12'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qwe" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1QWE 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=1QWE OCA].
__TOC__
 
</StructureSection>
==Reference==
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]
[[Category: Avian sarcoma virus]]
[[Category: Avian sarcoma virus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Transferase]]
[[Category: Chiyoshi K]]
[[Category: Chiyoshi, K.]]
[[Category: Feng S]]
[[Category: Feng, S.]]
[[Category: Rickles RJ]]
[[Category: Rickles, R J.]]
[[Category: Schreiber SL]]
[[Category: Schreiber, S L.]]
[[Category: class ii ligand complex]]
[[Category: src sh3 domain]]
 
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