|Title||The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex.|
|Publication Type||Journal Article|
|Year of Publication||2007|
|Authors||Candel, A. M., F. Conejero-Lara, J. C. Martinez, N. A. J. van Nuland, and M. Bruix|
|Date Published||2007 Feb 20|
|Keywords||Amino Acid Sequence, Animals, Chickens, Cross-Linking Reagents, Entropy, Ligands, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Mimicry, Peptides, Protein Binding, Recombinant Fusion Proteins, Spectrin, src Homology Domains|
Here we present the high-resolution NMR structure of a chimera (SPCp41) between alpha-spectrin SH3 domain and the decapeptide p41. The tertiary structure mimics perfectly the interactions typically found in SH3-peptide complexes and is remarkably similar to that of the complex between the separate Spc-SH3 domain and ligand p41. Relaxation data confirm the tight binding between the ligand and SH3 part of the chimera. This chimera will serve as a tool for a deeper understanding of the relationship between structure and thermodynamics of binding using a combination of NMR, stability and site-directed mutagenesis studies, which can lead to an effective strategy for ligand design.
|Alternate Journal||FEBS Lett.|