ArticleStructure (London, England : 1993)2005
Structural basis of affinity maturation and intramolecular cooperativity in a protein-protein interaction.
Article in Structure (London, England : 1993), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- In Vitro Detection of Biologically Active Staphylococcal Enterotoxins Type B and C1 as an Alternative to In Vivo Testing.Microorganisms · 2026Article
- Modifying inhibitor specificity for homologous enzymes by machine learning.The FEBS journal · 2026Article
- Structural convergence and water-mediated substrate mimicry enable broad neuraminidase inhibition by human antibodies.Nature communications · 2025Article
- Blocking Superantigen-Mediated Diseases: Challenges and Future Trends.Journal of immunology research · 2024Review
- Climbing Up and Down Binding Landscapes through Deep Mutational Scanning of Three Homologous Protein-Protein Complexes.Journal of the American Chemical Society · 2021Article
- Review
- Quantitative mapping of binding specificity landscapes for homologous targets by using a high-throughput method.The Biochemical journal · 2020Article
- Surprisingly Fast Interface and Elbow Angle Dynamics of Antigen-Binding Fragments.Frontiers in molecular biosciences · 2020Article
- Deciphering evolution of immune recognition in antibodies.BMC structural biology · 2018Article
- Resurrecting ancestral structural dynamics of an antiviral immune receptor: adaptive binding pocket reorganization repeatedly shifts RNA preference.BMC evolutionary biology · 2016Article
- Two common structural motifs for TCR recognition by staphylococcal enterotoxins.Scientific reports · 2016Article
- Structure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.PloS one · 2015Article
- Review
- Engineering a soluble high-affinity receptor domain that neutralizes staphylococcal enterotoxin C in rabbit models of disease.Protein engineering, design & selection : PEDS · 2013Article
- Structure-based rational design of a Toll-like receptor 4 (TLR4) decoy receptor with high binding affinity for a target protein.PloS one · 2012Article
- Clarifying the mechanism of superantigen toxicity.PLoS biology · 2011Article
- Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain.The Journal of biological chemistry · 2011Article
- A conserved hydrophobic patch on Vβ domains revealed by TCRβ chain crystal structures: Implications for pre-TCR dimerization.Frontiers in immunology · 2011Article
- Assessing energetic contributions to binding from a disordered region in a protein-protein interaction .Biochemistry · 2010Article
- Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC.Proteins · 2009Article
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9 authors.
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Abstract
Although protein-protein interactions are involved in nearly all cellular processes, general rules for describing affinity and selectivity in protein-protein complexes are lacking, primarily because correlations between changes in protein structure and binding energetics have not been well determined. Here, we establish the structural basis of affinity maturation for a protein-protein interaction system that we had previously characterized energetically. This model system exhibits a 1500-fold affinity increase. Also, its affinity maturation is restricted by negative intramolecular cooperativity. With three complex and six unliganded variant X-ray crystal structures, we provide molecular snapshots of protein interface remodeling events that span the breadth of the affinity maturation process and present a comprehensive structural view of affinity maturation. Correlating crystallographically observed structural changes with measured energetic changes reveals molecular bases for affinity maturation, intramolecular cooperativity, and context-dependent binding.
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