2O88
Crystal structure of the N114A mutant of ABL-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions
Summary for 2O88
| Entry DOI | 10.2210/pdb2o88/pdb |
| Related | 1BBZ |
| Descriptor | Proto-oncogene tyrosine-protein kinase ABL1, P41 peptide, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | sh3 domain high affinity peptide complex, signaling protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm, cytoskeleton. Isoform IB: Nucleus membrane; Lipid-anchor: P00519 |
| Total number of polymer chains | 4 |
| Total formula weight | 15022.53 |
| Authors | Camara-Artigas, A. (deposition date: 2006-12-12, release date: 2007-05-01, Last modification date: 2024-10-30) |
| Primary citation | Camara-Artigas, A.,Palencia, A.,Martinez, J.C.,Luque, I.,Gavira, J.A.,Garcia-Ruiz, J.M. 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. Acta Crystallogr.,Sect.D, 63:646-652, 2007 Cited by PubMed Abstract: 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. PubMed: 17452790DOI: 10.1107/S0907444907011109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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