ArticleJournal of the American Chemical Society2016
Side-Chain Conformational Preferences Govern Protein-Protein Interactions.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- An end-to-end deep learning method for protein side-chain packing and inverse folding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Sequence Tendency for the Interaction between Low-Complexity Intrinsically Disordered Proteins.JACS Au · 2023Article
- Exploiting Sequence-Dependent Rotamer Information in Global Optimization of Proteins.The journal of physical chemistry. B · 2022Article
- Anchor Residues Govern Binding and Folding of an Intrinsically Disordered Domain.ACS chemical biology · 2022Article
- Promiscuity mapping of the S100 protein family using a high-throughput holdup assay.Scientific reports · 2022Article
- Peptide Tethering: Pocket-Directed Fragment Screening for Peptidomimetic Inhibitor Discovery.Journal of the American Chemical Society · 2022Article
- Article
- Proteomimetic surface fragments distinguish targets by function.Chemical science · 2020Article
- Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.Peptide science (Hoboken, N.J.) · 2020Article
- Targeting the Side-Chain Convergence of Hydrophobic α-Helical Hot Spots To Design Small-Molecule Mimetics: Key Binding Features forJournal of medicinal chemistry · 2019Article
- Heterozygous Variants in KMT2E Cause a Spectrum of Neurodevelopmental Disorders and Epilepsy.American journal of human genetics · 2019Article
- Engineered protein scaffolds as leads for synthetic inhibitors of protein-protein interactions.Current opinion in chemical biology · 2018Review
- Rotamer Libraries for the High-Resolution Design of β-Amino Acid Foldamers.Structure (London, England : 1993) · 2017Article
- MFPred: Rapid and accurate prediction of protein-peptide recognition multispecificity using self-consistent mean field theory.PLoS computational biology · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
Protein secondary structures serve as geometrically constrained scaffolds for the display of key interacting residues at protein interfaces. Given the critical role of secondary structures in protein folding and the dependence of folding propensities on backbone dihedrals, secondary structure is expected to influence the identity of residues that are important for complex formation. Counter to this expectation, we find that a narrow set of residues dominates the binding energy in protein-protein complexes independent of backbone conformation. This finding suggests that the binding epitope may instead be substantially influenced by the side-chain conformations adopted. We analyzed side-chain conformational preferences in residues that contribute significantly to binding. This analysis suggests that preferred rotamers contribute directly to specificity in protein complex formation and provides guidelines for peptidomimetic inhibitor design.
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