Claim · model-written summary
A second domain was predicted to form a zipper-like coiled-coil.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianae1 - Outcome
- zipper-like coiled-coil structuree0
Not reportedMaterialGeneCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“A second domain is predicted to form a zipper-like coiled-coil structure.”
e1“from Arabidopsis thaliana”
Title
Dierk Wanke; Mareike L. Hohenstatt; Marek Dynowski; et al. PLoS ONE 2011. doi:10.1371/journal.pone.0016070
Other claims from this paper (7)
- Observation Ortholog comparison found two conserved signatures beyond the DNA binding domain.
- Mechanism A peptide signature was essential and sufficient for AtBPC6 nuclear and nucleolar targeting.
- Observation The domain resembles leucine zippers and contains alanines with seven-amino-acid heptad spacing.
- Mechanism The alanine zipper was essential for homotypic dimerization of group II proteins in vivo.
- Mechanism Predicted salt bridges and hydrogen bonds form an interaction domain differing from the classical zipper model.
- Method / resource FRET-FLIM validated parallel dimer formation in planta.
- Observation The domain was found across all kingdoms beyond BBR/BPC proteins.