Structural Basis of a Phototropin Light Switch

By S. Harper, L. Neil, Kevin Gardner. Science, 2003

763 citations recorded by the source corpus.

Subfields: Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/45eab645244e9ca05ce4289843a1a18e94dd0387

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Citations in the corpus

Light signal transduction in higher plants. (2004, background): “However, a recent NMR study of an oat phototropin construct containing the LOV2 domain with a 40 amino-acid carboxy-terminal extension (the linker helix between the LOV2 domain and the protein kinase domain) indicates a large light-driven structural rearrangement (70).”
Light-regulated plant growth and development. (2010, background): “Light-induced changes of the chromophore lead to structural changes of the protein initiating photoreceptor-mediated signal transduc tion (e.g., Harper et al., 2003; Pfeifer et al., 2010).”
Phytochrome structure and signaling mechanisms. (2006, background): “PAS and GAF domains are present in other signaling molecules; for example, the photosensory LOV domains of the phototropins are PAS domains (19, 37), whereas GAF domains have been implicated as regulators of cyclic nucleotide metabolism in organisms as diverse as cyanobacteria and mammals (62, 63).”
Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain (2010, background): “The C-terminal helical extensions of a PAS domain from the plant photoreceptor phototropin (40) and theDrosophila clock protein Period (41) and the N-terminal extension of a PAS domain in the fungal photoreceptor Vivid (42) all pack against the PAS core of the protein in a position similar to that o”
Light as a Growth Regulator: Controlling Plant Biology with Narrow-bandwidth Solid-state Lighting Systems (2008, background): “On absorption of a photon, the receptor undergoes a physical rearrangement that presents the kinase domain for catalysis (Christie et al., 2007; Harper et al., 2003).”
Engineering an improved light-induced dimer (iLID) for controlling the localization and activity of signaling proteins (2014, background): “Upon blue light irradiation, a conserved cysteine residue in the core of AsLOV2 becomes covalently bound to the flavin cofactor, structural rearrangement is passed along through the PAS fold, and ultimately the flanking helices unfold from the PAS core (11, 12).”
Protein sectors: evolutionary units of three-dimensional structure (2009, background): “Two sectors are also evident in the Per/Arnt/Sim (PAS) domain family of allosteric signaling modules in which ligand binding (or chromophore isomerisation) at a surface pocket located on one side triggers conformational changes at N- and C-terminal structural motifs docked at the opposite surface (H”