ArticleJournal of biomolecular NMR2011
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 56 citations in OpenAlex.
- Phosphorylation in the dynein light intermediate chain 2 isoform enables Pin1 binding and modulates cargo-adaptor interactions.Journal of structural biology: X · 2026Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- Glycan Stability and Flexibility: Thermodynamic and Kinetic Characterization of Nonconventional Hydrogen Bonding in Lewis Antigens.Journal of the American Chemical Society · 2023Article
- Impact of distant peptide substrate residues on enzymatic activity of SlyD.Cellular and molecular life sciences : CMLS · 2022Article
- Roles of peptidyl prolyl isomerase Pin1 in viral propagation.Frontiers in cell and developmental biology · 2022Review
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- Rapid Quantification of Protein-Ligand Binding viaBiophysical journal · 2020Article
- NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Two-dimensional NMR lineshape analysis of single, multiple, zero and double quantum correlation experiments.Journal of biomolecular NMR · 2020Article
- NmrLineGuru: Standalone and User-Friendly GUIs for Fast 1D NMR Lineshape Simulation and Analysis of Multi-State Equilibrium Binding Models.Scientific reports · 2019Article
- Tuning a timing device that regulates lateral root development in rice.Journal of biomolecular NMR · 2019Article
- Mechanisms of Specific versus Nonspecific Interactions of Aggregation-Prone Inhibitors and Attenuators.Journal of medicinal chemistry · 2019Article
- Quantification of reaction cycle parameters for an essential molecular switch in an auxin-responsive transcription circuit in rice.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Molecular Mechanism of the Pin1-Histone H1 Interaction.Biochemistry · 2019Article
- Free energy landscape remodeling of the cardiac pacemaker channel explains the molecular basis of familial sinus bradycardia.The Journal of biological chemistry · 2017Article
- Networks of Dynamic Allostery Regulate Enzyme Function.Structure (London, England : 1993) · 2017Article
- Cyclic cis-Locked Phospho-Dipeptides Reduce Entry of AβPP into Amyloidogenic Processing Pathway.Journal of Alzheimer's disease : JAD · 2017Article
- Neighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding.The FEBS journal · 2016Article
- Two-Dimensional NMR Lineshape Analysis.Scientific reports · 2016Article
- Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1.Structure (London, England : 1993) · 2015Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation, rigorous enzymatic assays of isomerization are required. However, most measures of isomerase activity require significant constraints on substrate sequence and only yield rate constants for the cis isomer, [Formula: see text] and apparent Michaelis constants, [Formula: see text]. By contrast, NMR lineshape analysis is a powerful tool for determining microscopic rates and populations of each state in a complex binding scheme. The isolated catalytic domain of Pin1 was employed as a first step towards elucidating the reaction scheme of the full-length enzyme. A 24-residue phosphopeptide derived from the amyloid precurser protein intracellular domain (AICD) phosphorylated at Thr668 served as a biologically-relevant Pin1 substrate. Specific (13)C labeling at the Pin1-targeted proline residue provided multiple reporters sensitive to individual isomer binding and on-enzyme catalysis. We have performed titration experiments and employed lineshape analysis of phosphopeptide (13)C-(1)H constant time HSQC spectra to determine [Formula: see text], [Formula: see text], [Formula: see text], and [Formula: see text] for the catalytic domain of Pin1 acting on this AICD substrate. The on-enzyme equilibrium value of [E·trans]/[E·cis] = 3.9 suggests that the catalytic domain of Pin1 is optimized to operate on this substrate near equilibrium in the cellular context. This highlights the power of lineshape analysis for determining the microscopic parameters of enzyme catalysis, and demonstrates the feasibility of future studies of Pin1-PPIase mutants to gain insights on the catalytic mechanism of this important enzyme.
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