The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex.

TitleThe high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex.
Publication TypeJournal Article
Year of Publication2007
AuthorsCandel, A. M., F. Conejero-Lara, J. C. Martinez, N. A. J. van Nuland, and M. Bruix
JournalFEBS Lett
Volume581
Issue4
Pagination687-92
Date Published2007 Feb 20
ISSN0014-5793
KeywordsAmino 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
Abstract

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.

DOI10.1016/j.febslet.2007.01.032
Alternate JournalFEBS Lett.
PubMed ID17275816