Cargando…
The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3
BACKGROUND: SH3 domains are small protein modules of 60–85 amino acids that bind to short proline-rich sequences with moderate-to-low affinity and specificity. Interactions with SH3 domains play a crucial role in regulation of many cellular processes (some are related to cancer and AIDS) and have th...
Autores principales: | Casares, Salvador, AB, Eiso, Eshuis, Henk, Lopez-Mayorga, Obdulio, van Nuland, Nico AJ, Conejero-Lara, Francisco |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1853097/ https://www.ncbi.nlm.nih.gov/pubmed/17407569 http://dx.doi.org/10.1186/1472-6807-7-22 |
Ejemplares similares
-
Distinct Ubiquitin Binding Modes Exhibited by SH3 Domains: Molecular Determinants and Functional Implications
por: Ortega Roldan, Jose L., et al.
Publicado: (2013) -
Autoinhibition of Bcr-Abl through Its SH3 Domain
por: Smith, Kristen M., et al.
Publicado: (2003) -
SH2 and SH3 domains
por: Pawson, Tony
Publicado: (1992) -
Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex
por: Ortega-Roldan, Jose Luis, et al.
Publicado: (2009) -
Multi-Timescale Conformational Dynamics of the SH3 Domain of CD2-Associated Protein using NMR Spectroscopy and Accelerated Molecular Dynamics**
por: Salmon, Loïc, et al.
Publicado: (2012)