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The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex
Publication Type:
Journal ArticleSource:
Volume 581, Issue 4, p.687 - 692 (2007)URL:
PM:17275816Keywords:
Amino Acid Sequence; Animals; Chickens; Cross-Linking Reagents; pharmacology; Entropy; Ligands; Magnetic Resonance Spectroscopy; Models; Molecular; Molecular Mimicry; drug effects; Peptides; chemistry; Protein Binding; Recombinant Fusion Proteins; SpectrinAbstract:
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
Notes:
DA - 20070213
IS - 0014-5793 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Cross-Linking Reagents)
RN - 0 (Ligands)
RN - 0 (Peptides)
RN - 0 (Recombinant Fusion Proteins)
RN - 12634-43-4 (Spectrin)
SB - IM