ArticleJournal of molecular biology2011
Structure of an enclosed dimer formed by the Drosophila period protein.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Genomic Signatures of Speciation in Butterflies.Systematic biology · 2026Article
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Clock gene homologs lin-42 and kin-20 regulate circadian rhythms in C. elegans.Scientific reports · 2024Article
- Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022Review
- Circadian Oscillators: Around the Transcription-Translation Feedback Loop and on to Output.Trends in biochemical sciences · 2016Review
- Signal Transduction by BvgS Sensor Kinase: BINDING OF MODULATOR NICOTINATE AFFECTS THE CONFORMATION AND DYNAMICS OF THE ENTIRE PERIPLASMIC MOIETY.The Journal of biological chemistry · 2015Article
- The PXDLS linear motif regulates circadian rhythmicity through protein-protein interactions.Nucleic acids research · 2014Article
- Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides.Acta crystallographica. Section D, Biological crystallography · 2014Article
- bHLH-PAS proteins in cancer.Nature reviews. Cancer · 2013Review
- Structure and dimerization properties of the aryl hydrocarbon receptor PAS-A domain.Molecular and cellular biology · 2013Article
- Rare variants in single-minded 1 (SIM1) are associated with severe obesity.The Journal of clinical investigation · 2013Article
- Light-induced subunit dissociation by a light-oxygen-voltage domain photoreceptor from Rhodobacter sphaeroides.Biochemistry · 2013Article
- Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex.Science (New York, N.Y.) · 2012Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Period (PER) is the major transcription inhibitor in metazoan circadian clocks and lies at the center of several feedback loops that regulate gene expression. Dimerization of Drosophila PER influences nuclear translocation, repressor activity, and behavioral rhythms. The structure of a central, 346-residue PER fragment reveals two associated PAS (Per-Arnt-Sim) domains followed by a protruding α-helical extension (αF). A closed, pseudo-symmetric dimer forms from a cross handshake interaction of the N-terminal PAS domain with αF of the opposing subunit. Strikingly, a shift of αF against the PAS β-sheet generates two alternative subunit interfaces in the dimer. Taken together with a previously reported PER structure in which αF extends, these data indicate that αF unlatches to switch association of PER with itself to its partner Timeless. The variable positions of the αF helix provide snapshots of a helix dissociation mechanism that has relevance to other PAS protein systems. Conservation of PER interaction residues among a family of PAS-AB-containing transcription factors suggests that contacts mediating closed PAS-AB dimers serve a general function.
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