TY  - GEN 
AU  - Casares Atienza, Salvador
AU  - AB, Eiso
AU  - Eshuis, Henk
AU  - López-Mayorga, Obdulio
AU  - AJ van Nuland, Nico
AU  - Conejero Lara, Francisco
PY  - 2007
SN  - 1472-6807
UR  - http://hdl.handle.net/10481/32745
AB  - [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...
AB  - [Results]

Here we present the high-resolution structure of the complex between the R21A mutant of Spc-SH3 and p41 derived from NMR data. Thermodynamic parameters of binding of p41 to both WT and R21A Spc-SH3 were measured by a combination of...
AB  - [Conclusion]

Based on a deep structural and thermodynamic analysis of a low and high affinity complex of two different SH3 domains with the same ligand p41, we underline the importance of taking into account in any effective strategy of rational...
LA  - eng
PB  - Biomed Central
KW  - Proteins
KW  - Peptides
KW  - Intersectin 1
KW  - α-spectrin
KW  - AIRs
KW  - Neuregulin 1
TI  - The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3
DO  - 10.1186/1472-6807-7-22
ER  -