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dc.contributor.authorBosch Presegué, Laia
dc.contributor.authorIarriccio Silva, Laura
dc.contributor.authorAguila Cerda, Mónica
dc.contributor.authorToledo, Darwin
dc.contributor.authorRamon Portés, Eva
dc.contributor.authorCordomí Montoya, Arnau
dc.contributor.authorGarriga Solé, Pere
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2011-09-19T11:07:52Z
dc.date.available2011-09-19T11:07:52Z
dc.date.created2011-02-15
dc.date.issued2011-02-15
dc.identifier.citationBosch [et al.]. Hydrophobic amino acids at the cytoplasmic ends of helices 3 and 6 of rhodopsin conjointly modulate transducin activation. "Archives of biochemistry and biophysics", 15 Febrer 2011, vol. 506, núm. 2, p. 142-149.
dc.identifier.issn0003-9861
dc.identifier.urihttp://hdl.handle.net/2117/13237
dc.description.abstractRhodopsin is the visual photoreceptor responsible for dim light vision. This receptor is located in the rod cell of the retina and is a prototypical member of the G-protein-coupled receptor superfamily. The structural details underlying the molecular recognition event in transducin activation by photoactivated rhodopsin are of key interest to unravel the molecular mechanism of signal transduction in the retina. We constructed and expressed rhodopsin mutants in the second and third cytoplasmic domains of rhodopsin –where the natural amino acids were substituted by the human M3 acetylcholine muscarinic receptor homologous residues– in order to determine their potential involvement in G-protein recognition. These mutants showed normal chromophore formation and a similar photobleaching behavior than WT rhodopsin, but decreased thermal stability in the dark state. The single mutant V1383.53 and the multiple mutant containing V2275.62 and a combination of mutations at the cytoplasmic end of transmembrane helix 6 caused a reduction in transducin activation upon rhodopsin photoactivation. Furthermore, combination of mutants at the second and third cytoplasmic domains revealed a cooperative role, and partially restored transducin activation. The results indicate that hydrophobic interactions by V1383.53, V2275.62, V2506.33, V2546.37 and I2556.38 are critical for receptor activation and/or efficient rhodopsin–transducin interaction.
dc.format.extent8 p.
dc.language.isoeng
dc.subjectÀrees temàtiques de la UPC::Enginyeria química::Biotecnologia
dc.subject.lcshRhodopsin
dc.subject.lcshVisual phototransduction
dc.subject.lcshG proteins -- Receptors
dc.titleHydrophobic amino acids at the cytoplasmic ends of helices 3 and 6 of rhodopsin conjointly modulate transducin activation
dc.typeArticle
dc.subject.lemacFototransducció visual
dc.subject.lemacProteïnes G -- Receptors
dc.contributor.groupUniversitat Politècnica de Catalunya. GBMI - Grup de Biotecnologia Molecular i Industrial
dc.identifier.doi10.1016/j.abb.2010.11.019
dc.description.peerreviewedPeer Reviewed
dc.rights.accessRestricted access - publisher's policy
local.identifier.drac5352252
dc.description.versionPostprint (published version)
local.citation.authorBosch; Iarriccio, L.; Aguila, M.; Toledo, D.; Ramon, E.; Cordomí, A.; Garriga, P.
local.citation.publicationNameArchives of biochemistry and biophysics
local.citation.volume506
local.citation.number2
local.citation.startingPage142
local.citation.endingPage149


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