ArticleJournal of the American Chemical Society2016
Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling.
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 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- The Molecular Chaperone Mechanism of the C-Terminal Domain of Large-Size Subunit Catalases.Antioxidants (Basel, Switzerland) · 2023Article
- The interactions of molecular chaperones with client proteins: why are they so weak?The Journal of biological chemistry · 2021Review
- Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.mBio · 2021Article
- Molecular chaperones and their denaturing effect on client proteins.Journal of biomolecular NMR · 2021Article
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- The Anti-Aggregation Holdase Hsp33 Promotes the Formation of Folded Protein Structures.Biophysical journal · 2020Article
- Identifying dynamic, partially occupied residues using anomalous scattering.Acta crystallographica. Section D, Structural biology · 2019Article
- Protein folding while chaperone bound is dependent on weak interactions.Nature communications · 2019Article
- The molecular basis of chaperone-mediated interleukin 23 assembly control.Nature communications · 2019Article
- Reply to 'Misreading chaperone-substrate complexes from random noise'.Nature structural & molecular biology · 2018Article
- Directed evolution to improve protein folding in vivo.Current opinion in structural biology · 2018Review
- Folding while bound to chaperones.Current opinion in structural biology · 2018Review
- Selecting Conformational Ensembles Using Residual Electron and Anomalous Density (READ).Methods in molecular biology (Clifton, N.J.) · 2018Article
- The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants.Protein science : a publication of the Protein Society · 2017Article
- Chaperone-client interactions: Non-specificity engenders multifunctionality.The Journal of biological chemistry · 2017Review
- Visualizing chaperone-assisted protein folding.Nature structural & molecular biology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Chaperones maintain a healthy proteome by preventing aggregation and by aiding in protein folding. Precisely how chaperones influence the conformational properties of their substrates, however, remains unclear. To achieve a detailed description of dynamic chaperone-substrate interactions, we fused site-specific NMR information with coarse-grained simulations. Our model system is the binding and folding of a chaperone substrate, immunity protein 7 (Im7), with the chaperone Spy. We first used an automated procedure in which NMR chemical shifts inform the construction of system-specific force fields that describe each partner individually. The models of the two binding partners are then combined to perform simulations on the chaperone-substrate complex. The binding simulations show excellent agreement with experimental data from multiple biophysical measurements. Upon binding, Im7 interacts with a mixture of hydrophobic and hydrophilic residues on Spy's surface, causing conformational exchange within Im7 to slow down as Im7 folds. Meanwhile, the motion of Spy's flexible loop region increases, allowing for better interaction with different substrate conformations, and helping offset losses in Im7 conformational dynamics that occur upon binding and folding. Spy then preferentially releases Im7 into a well-folded state. Our strategy has enabled a residue-level description of a dynamic chaperone-substrate interaction, improving our understanding of how chaperones facilitate substrate folding. More broadly, we validate our approach using two other binding partners, showing that this approach provides a general platform from which to investigate other flexible biomolecular complexes through the integration of NMR data with efficient computational models.
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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.