The structural and energetic basis for high selectivity in a high-affinity protein-protein interaction.

Journal article

High-affinity, high-selectivity protein-protein interactions that are critical for cell survival present an evolutionary paradox: How does selectivity evolve when acquired mutations risk a lethal loss of high-affinity binding? A detailed understanding of selectivity in such complexes requires structural information on weak, noncognate complexes which can be difficult to obtain due to their transient and dynamic nature. Using NMR-based docking as a guide, we deployed a disulfide-trapping strat...

Expand abstract

Authors: Meenan, N; Sharma, A; Fleishman, S; Macdonald, C; Morel, B

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 107
• Issue: 22
• Pages: 10080-10085
• Publication date: 2010-06-01
• DOI: 10.1073/pnas.0910756107
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Endodeoxyribonucleases; Recombinant Proteins; Amino Acid Substitution; Models, Molecular; Crystallography, X-Ray; Mutagenesis, Site-Directed; Disulfides; Nuclear Magnetic Resonance, Biomolecular; Thermodynamics; Colicins; Molecular Sequence Data; Sequence Homology, Amino Acid; Multiprotein Complexes; Binding Sites; Protein Interaction Domains and Motifs; Amino Acid Sequence