ArticleAngewandte Chemie (International ed. in English)2020
Protein Allostery at Atomic Resolution.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Newton's cradle-like allosteric mechanism explains regulatory RsmE RNA binding.Nature communications · 2026Article
- Restraining Interproton Angular and Distance Dynamics with KEnRef.The journal of physical chemistry. B · 2026Article
- Insights into mechanisms of MALT1 allostery from NMR and AlphaFold dynamic analyses.Communications biology · 2024Article
- Targeting SHP2 Cryptic Allosteric Sites for Effective Cancer Therapy.International journal of molecular sciences · 2024Article
- The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis.Scientific data · 2024Article
- Water irradiation devoid pulses enhance the sensitivity ofJournal of biomolecular NMR · 2023Article
- Integrated approaches for the recognition of small molecule inhibitors for Toll-like receptor 4.Computational and structural biotechnology journal · 2023Article
- Atomic resolution protein allostery from the multi-state structure of a PDZ domain.Nature communications · 2022Article
- Advances in the exact nuclear Overhauser effect 2018-2022.Methods (San Diego, Calif.) · 2022Review
- On the use of residual dipolar couplings in multi-state structure calculation of two-domain proteins.Magnetic resonance letters · 2022Article
- Optimization and validation of multi-state NMR protein structures using structural correlations.Journal of biomolecular NMR · 2022Article
- High ResolutionFrontiers in molecular biosciences · 2022Review
- Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance.Journal of the American Chemical Society · 2021Article
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Authors and funding
11 authors.
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Abstract
Protein allostery is a phenomenon involving the long range coupling between two distal sites in a protein. In order to elucidate allostery at atomic resoluion on the ligand-binding WW domain of the enzyme Pin1, multistate structures were calculated from exact nuclear Overhauser effect (eNOE). In its free form, the protein undergoes a microsecond exchange between two states, one of which is predisposed to interact with its parent catalytic domain. In presence of the positive allosteric ligand, the equilibrium between the two states is shifted towards domain-domain interaction, suggesting a population shift model. In contrast, the allostery-suppressing ligand decouples the side-chain arrangement at the inter-domain interface thereby reducing the inter-domain interaction. As such, this mechanism is an example of dynamic allostery. The presented distinct modes of action highlight the power of the interplay between dynamics and function in the biological activity of proteins.
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