ArticleProceedings of the National Academy of Sciences of the United States of America2009
ARNT PAS-B has a fragile native state structure with an alternative beta-sheet register nearby in sequence space.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Measuring radiofrequency fields in NMR spectroscopy using offset-dependent nutation profiles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2021Article
- Structural insight into the role of the PAS domainfor signal transduction in sensor-kinase BvgS.Journal of bacteriology · 2021Article
- Reconstruction of ARNT PAS-B Unfolding Pathways by Steered Molecular Dynamics and Artificial Neural Networks.Journal of chemical theory and computation · 2021Article
- Volume and compressibility differences between protein conformations revealed by high-pressure NMR.Biophysical journal · 2021Article
- High-pressure NMR measurements provide insights into the different structural states that proteins can adopt.Biophysical journal · 2021Article
- Fragile protein folds: Sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations.Magnetic resonance (Gottingen, Germany) · 2021Article
- Ligand-induced perturbation of the HIF-2α:ARNT dimer dynamics.PLoS computational biology · 2018Article
- Conformational Changes of an Interdomain Linker Mediate Mechanical Signal Transmission in Sensor Kinase BvgS.Journal of bacteriology · 2017Article
- Article
- Ah Receptor Pathway Intricacies; Signaling Through Diverse Protein Partners and DNA-Motifs.Toxicology research · 2015Article
- Observed octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native "ball-and-socket" interacting residues by an affinity tag.Protein science : a publication of the Protein Society · 2013Article
- Characterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmission.BMC microbiology · 2013Article
- Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.Biophysical journal · 2012Article
- Direct observations of shifts in the β-sheet register of a protein-peptide complex using explicit solvent simulations.Biophysical journal · 2011Article
- Proteins that switch folds.Current opinion in structural biology · 2010Review
- An alternative conformation of the T-cell receptor alpha constant region.Journal of molecular biology · 2010Article
- Structure and signaling mechanism of Per-ARNT-Sim domains.Structure (London, England : 1993) · 2009Review
- Slow transition between two beta-strand registers is dictated by protein unfolding.Journal of the American Chemical Society · 2009Article
- Delineating the conformational elements responsible for Cu(2+)-induced oligomerization of beta-2 microglobulin.Biochemistry · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The aryl hydrocarbon receptor nuclear translocator (ARNT) is a basic helix-loop-helix Period/ARNT/Single-minded (bHLH-PAS) protein that controls various biological pathways as part of dimeric transcriptional regulator complexes with other bHLH-PAS proteins. The two PAS domains within ARNT, PAS-A and PAS-B, are essential for the formation of these complexes because they mediate protein-protein interactions via residues located on their beta-sheet surfaces. While investigating the importance of residues in ARNT PAS-B involved in these interactions, we uncovered a point mutation (Y456T) on the solvent-exposed beta-sheet surface that allowed this domain to interconvert with a second, stable conformation. Although both conformations are present in equivalent quantities in the Y456T mutant, this can be shifted almost completely to either end point by additional mutations. A high-resolution solution structure of a mutant ARNT PAS-B domain stabilized in the new conformation revealed a 3-residue slip in register and accompanying inversion of the central Ibeta-strand. We have demonstrated that the new conformation has >100-fold lower in vitro affinity for its heterodimerization partner, hypoxia-inducible factor 2alpha PAS-B. We speculate that the pliability in beta-strand register is related to the flexibility required of ARNT to bind to several partners and, more broadly, to the abilities of some PAS domains to regulate their activities in response to small-molecule cofactors.
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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.