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 ==Crystal structure of the ABL-SH3 domain complexed with the designed high-affinity peptide ligand P17==
 <StructureSection load='4j9i' size='340' side='right' caption='[[4j9i]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABL, ABL1, JTK7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_protein-tyrosine_kinase Non-specific protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.2 2.7.10.2] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j9i RCSB], [http://www.ebi.ac.uk/pdbsum/4j9i PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9i OCA], [http://pdbe.org/4j9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j9i RCSB], [http://www.ebi.ac.uk/pdbsum/4j9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9i ProSAT]</span></td></tr>
 </table>
 == Disease ==
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 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-The recognition of proline-rich ligands by SH3 domains is part of the process leading to diseases such as cancer or AIDS. Understanding the molecular determinants of the binding affinity and specificity of these interactions is crucial for the development of potent inhibitors with therapeutic potential. In this study, the crystallographic structure of the N114A mutant of the SH3 domain of the Abelson leukaemia virus tyrosine kinase complexed with a high-affinity peptide is presented. The crystallization was carried out using the capillary counter-diffusion technique, which facilitates the screening, manipulation and transport of the crystals and allows the collection of X-ray data directly from the capillary in which the crystals were grown. The crystals of the N114A mutant belong to the orthorhombic P2(1)2(1)2(1) space group, with unit-cell parameters a = 48.2, b = 50.1, c = 56.4 A. The quality of the diffraction data set has allowed the structure of the complex to be determined at a resolution limit of 1.75 A.
+The interaction of Abl-Src homology 3 domain (SH3) with the high affinity peptide p41 is the most notable example of the inconsistency existing between the currently accepted description of SH3 complexes and their binding thermodynamic signature. We had previously hypothesized that the presence of interfacial water molecules is partially responsible for this thermodynamic behavior. We present here a thermodynamic, structural, and molecular dynamics simulation study of the interaction of p41 with Abl-SH3 and a set of mutants designed to alter the water-mediated interaction network. Our results provide a detailed description of the dynamic properties of the interfacial water molecules and a molecular interpretation of the thermodynamic effects elicited by the mutations in terms of the modulation of the water-mediated hydrogen bond network. In the light of these results, a new dual binding mechanism is proposed that provides a better description of proline-rich ligand recognition by Abl-SH3 and that has important implications for rational design.
-Crystallization by capillary counter-diffusion and structure determination of the N114A mutant of the SH3 domain of Abl tyrosine kinase complexed with a high-affinity peptide ligand.,Camara-Artigas A, Palencia A, Martinez JC, Luque I, Gavira JA, Garcia-Ruiz JM Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):646-52. Epub 2007, Apr 21. PMID:17452790<ref>PMID:17452790</ref>
+Role of interfacial water molecules in proline-rich ligand recognition by the Src homology 3 domain of Abl.,Palencia A, Camara-Artigas A, Pisabarro MT, Martinez JC, Luque I J Biol Chem. 2010 Jan 22;285(4):2823-33. Epub 2009 Nov 10. PMID:19906645<ref>PMID:19906645</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4j9i" style="background-color:#fffaf0;"></div>
 ==See Also==