ArticleJournal of biomolecular NMR2009
Mapping the dynamics of ligand reorganization via 13CH3 and 13CH2 relaxation dispersion at natural abundance.
Article in Journal of biomolecular NMR, 2009. 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, 28 citations in OpenAlex.
- Mapping Phosphorylation-Specific Pin1-CRMP2 Interactions Using an Integrated Mass Spectrometry Approach.ACS chemical biology · 2026Article
- Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent.Biochemistry · 2024Article
- Protein Allostery at Atomic Resolution.Angewandte Chemie (International ed. in English) · 2020Article
- Allostery and Epistasis: Emergent Properties of Anisotropic Networks.Entropy (Basel, Switzerland) · 2020Article
- Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1.The journal of physical chemistry. B · 2018Article
- Label-free NMR-based dissociation kinetics determination.Journal of biomolecular NMR · 2017Article
- Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1.Molecules (Basel, Switzerland) · 2017Article
- Ligand-detected relaxation dispersion NMR spectroscopy: dynamics of preQ1-RNA binding.Angewandte Chemie (International ed. in English) · 2015Article
- Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.Scientific reports · 2013Article
- Interdomain interactions support interdomain communication in human Pin1.Biochemistry · 2013Article
- Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.Journal of biomolecular NMR · 2011Article
- Stereospecific gating of functional motions in Pin1.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Toward flexibility-activity relationships by NMR spectroscopy: dynamics of Pin1 ligands.Journal of the American Chemical Society · 2010Article
- A topical issue: NMR investigations of molecular dynamics.Journal of biomolecular NMR · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Flexible ligands pose challenges to standard structure-activity studies since they frequently reorganize their conformations upon protein binding and catalysis. Here, we demonstrate the utility of side chain (13)C relaxation dispersion measurements to identify and quantify the conformational dynamics that drive this reorganization. The dispersion measurements probe methylene (13)CH(2) and methyl (13)CH(3) groups; the latter are highly prevalent side chain moieties in known drugs. Combining these side chain studies with existing backbone dispersion studies enables a comprehensive investigation of mus-ms conformational dynamics related to binding and catalysis. We perform these measurements at natural (13)C abundance, in congruence with common pharmaceutical research settings. We illustrate these methods through a study of the interaction of a phosphopeptide ligand with the peptidyl-prolyl isomerase, Pin1. The results illuminate the side-chain moieties that undergo conformational readjustments upon complex formation. In particular, we find evidence that multiple exchange processes influence the side chain dispersion profiles. Collectively, our studies illustrate how side-chain relaxation dispersion can shed light on ligand conformational transitions required for activity, and thereby suggest strategies for its optimization.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.