English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/18508
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


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

AuthorsCámara-Artigas, A.; Palencia, A.; Martínez, Jose C.; Luque, I.; Gavira Gallardo, J. A. ; García Ruiz, Juan Manuel
KeywordsSH3 domains
Capillary counter-diffusion
Abl tyrosine kinase
Issue DateMay-2007
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section D 63(5): 646-652 (2007)
AbstractThe 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 P212121 space group, with unit-cell parameters a = 48.2, b = 50.1, c = 56.4 Å. The quality of the diffraction data set has allowed the structure of the complex to be determined at a resolution limit of 1.75 Å.
Description7 pages, 5 figures, 1 table.
Publisher version (URL)http://dx.doi.org/10.1107/S0907444907011109
Appears in Collections:(IACT) Artículos
Files in This Item:
There are no files associated with this item.
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.