Biomaterial Database

Dark and photoactivated rhodopsin share common binding modes to transducin. 2008

Francesca Fanelli, and Daniele Dell'orco

Dulbecco Telethon Institute and Department of Chemistry, via Campi 183, 41100 Modena, Italy. fanelli@unimo.it <fanelli@unimo.it>

The structure of the photoactivated deprotonated rhodopsin intermediate was compared with two different structures of dark rhodopsin. Structure comparisons relied on the computation of molecular indices and on docking simulations with heterotrimeric transducin (Gt). The results of this study provide the first evidence that dark and photoactivated rhodopsins share a common recognition mode to Gt, characterized by the docking of the Gt alpha C-tail in the proximity to the E/DRY motif of rhodopsin.

UI	MeSH Term	Description	Entries
D008027	Light	That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.	Light, Visible,Photoradiation,Radiation, Visible,Visible Radiation,Photoradiations,Radiations, Visible,Visible Light,Visible Radiations
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D003624	Darkness	The absence of light.	Darknesses
D012243	Rhodopsin	A purplish-red, light-sensitive pigment found in RETINAL ROD CELLS of most vertebrates. It is a complex consisting of a molecule of ROD OPSIN and a molecule of 11-cis retinal (RETINALDEHYDE). Rhodopsin exhibits peak absorption wavelength at about 500 nm.	Visual Purple
D015293	Transducin	A heterotrimeric GTP-binding protein that mediates the light activation signal from photolyzed rhodopsin to cyclic GMP phosphodiesterase and is pivotal in the visual excitation process. Activation of rhodopsin on the outer membrane of rod and cone cells causes GTP to bind to transducin followed by dissociation of the alpha subunit-GTP complex from the beta/gamma subunits of transducin. The alpha subunit-GTP complex activates the cyclic GMP phosphodiesterase which catalyzes the hydrolysis of cyclic GMP to 5'-GMP. This leads to closure of the sodium and calcium channels and therefore hyperpolarization of the rod cells.	G-Protein, Inhibitory Gt,Gt, Transducin G-Protein,alpha-Transducin,beta-Transducin,gamma-Transducin,Transducin G-Protein (Gt),Transducin, alpha Subunit,Transducin, beta Subunit,Transducin, gamma Subunit,G Protein, Inhibitory Gt,G-Protein Gt, Transducin,Gt G-Protein, Inhibitory,Gt, Transducin G Protein,Inhibitory Gt G-Protein,Transducin G-Protein Gt,alpha Subunit Transducin,alpha Transducin,beta Subunit Transducin,beta Transducin,gamma Subunit Transducin,gamma Transducin