ArticleBiophysical journal2006
Dynamic switching mechanisms in LOV1 and LOV2 domains of plant phototropins.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed.
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Protein Electrostatics Tune the Singlet-Triplet Energy Gap in Natural and Engineered Phototropin Light-Oxygen-Voltage (LOV) Domains.Journal of the American Chemical Society · 2026Article
- Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- Disruption of the FMN-A524 interaction cascade and Glu513-induced collapse of the hydrophobic barrier promotes light-induced Jα-helix unfolding in AsLOV2.Biophysical journal · 2023Article
- Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine.Nature communications · 2022Article
- High-resolution structure and dynamics of mitochondrial complex I-Insights into the proton pumping mechanism.Science advances · 2021Article
- QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.Physical chemistry chemical physics : PCCP · 2021Article
- Computational Investigation of Structural and Spectroscopic Properties of LOV-Based Proteins with Improved Fluorescence.The journal of physical chemistry. B · 2021Article
- Toward Multiplexed Optogenetic Circuits.Frontiers in bioengineering and biotechnology · 2021Review
- Multiple Reaction Pathways in the Morphinone Reductase-Catalyzed Hydride Transfer Reaction.ACS omega · 2020Article
- New Light on the Mechanism of Phototransduction in Phototropin.Biochemistry · 2020Article
- A Noncanonical Chromophore Reveals Structural Rearrangements of the Light-Oxygen-Voltage Domain upon Photoactivation.Biochemistry · 2019Article
- Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase.Nature communications · 2017Article
- Role of water and protein dynamics in proton pumping by respiratory complex I.Scientific reports · 2017Article
- Regulation of neural gene transcription by optogenetic inhibition of the RE1-silencing transcription factor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics study.Journal of inorganic biochemistry · 2015Article
- Redox-induced activation of the proton pump in the respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- LOV-based optogenetic devices: light-driven modules to impart photoregulated control of cellular signaling.Frontiers in molecular biosciences · 2015Review
- Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations-implications for the understanding of LOV photoactivation.Frontiers in molecular biosciences · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
LOV domains are the light-sensitive portion of plant phototropins. They absorb light through a flavin cofactor, photochemically form a covalent bond between the chromophore and a cysteine residue in the protein, and proceed to mediate activation of an attached kinase domain. Although the photoreaction itself is now well-characterized experimentally and computationally, it is still unclear how the formation of the adduct leads to kinase activation. We have performed molecular dynamics simulations on the LOV1 domain of Chlamydomonas reinhardtii and the LOV2 domain of Avena sativa, both before and after the photoreaction, to answer this question. The extensive simulations, over 240 ns in duration, reveal significant differences in how the LOV1 and LOV2 domains respond to photoactivation. The simulations indicate that LOV1 activation is likely caused by a change in hydrogen bonding between protein and ligand that destabilizes a highly conserved salt bridge, whereas LOV2 activation seems to result from a change in the flexibility of a set of protein loops. Results of electrostatics calculations, principal component analysis, sequence alignments, and root mean-square deviation analysis corroborate the above findings.
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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.