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The high‐resolution NMR structure of a single‐chain chimeric protein mimicking a SH3–peptide complex
Author(s) -
Candel Adela M.,
Conejero-Lara Francisco,
Martinez Jose C.,
van Nuland Nico A.J.,
Bruix Marta
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.01.032
Subject(s) - chemistry , sh3 domain , chimera (genetics) , spectrin , peptide , ligand (biochemistry) , crystallography , nuclear magnetic resonance spectroscopy , biophysics , stereochemistry , biochemistry , receptor , biology , proto oncogene tyrosine protein kinase src , cytoskeleton , cell , gene
Here we present the high‐resolution NMR structure of a chimera (SPCp41) between α‐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.