Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity.

Biochemistry - 28 Dec 2004

Harper Shannon M, Christie John M, Gardner Kevin H

Abstract excerpt

Light plays a crucial role in activating phototropins, a class of plant photoreceptors that are sensitive to blue and UV-A wavelengths. Previous studies indicated that phototropin uses a bound flavin mononucleotide (FMN) within its light-oxygen-voltage (LOV) domain to generate a protein-flavin covalent bond under illumination. In the C-terminal LOV2 domain of Avena sativa phototropin 1, formation of this bond...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arabidopsis
Share to Arabidopsis Proteins
Share to Avena

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cryptochromes

Share to Flavoproteins

Share to Protein Kinases

Share to Protein Structure, Secondary

Share to Static Electricity

Source

Identifiers

PMID: 15610012
DOI: 10.1021/bi048092i

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity.PMID 15610012Read ↗

Signaling mechanisms of LOV domains: new insights from molecular dynamics studies.Semantic proximity Read ↗

Unraveling the Mechanism of a LOV Domain Optogenetic Sensor: A Glutamine Lever Induces Unfolding of the Jα Helix.Semantic proximity Read ↗

Light signal transduction pathway from flavin chromophore to the J alpha helix of Arabidopsis phototropin1.Semantic proximity Read ↗

TULIPs: tunable, light-controlled interacting protein tags for cell biology.Semantic proximity Read ↗

Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function.Semantic proximity Read ↗

Photochemically induced dynamic nuclear polarization in a C450A mutant of the LOV2 domain of the Avena sativa blue-light receptor phototropin.Semantic proximity Read ↗

Mechanism-based tuning of a LOV domain photoreceptor.Semantic proximity Read ↗

Engineering light-inducible nuclear localization signals for precise spatiotemporal control of protein dynamics in living cells.Semantic proximity Read ↗

Investigating models of protein function and allostery with a widespread mutational analysis of a light-activated protein.Semantic proximity Read ↗

Mutations in N-terminal flanking region of blue light-sensing light-oxygen and voltage 2 (LOV2) domain disrupt its repressive activity on kinase domain in the Chlamydomonas phototropin.Semantic proximity Read ↗

Time-resolved Fourier transform infrared study on photoadduct formation and secondary structural changes within the phototropin LOV domain.Semantic proximity Read ↗

The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.