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== Structure of TRPV1 == | == Structure of TRPV1 == | ||
The TRPV1 receptor is a transmembrane protein receptor. It is made up of '''839 amino acids'''. It’s molecular weight is '''94 938Da'''.<ref> | The TRPV1 receptor is a transmembrane protein receptor. It is made up of '''839 amino acids'''. It’s molecular weight is '''94 938Da'''.<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy">Liao, M., Cao, E., Julius, D., & Cheng, Y. (2013b). Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature, 504(7478), 107‑112. https://doi.org/10.1038/nature12822(consulté le déc. 28, 2020)</ref> TRPV1 exists in two states : the open state and the closed state.<ref> T. Rosenbaum et S. A. Simon, « TRPV1 Receptors and Signal Transduction », in TRP Ion Channel Function in Sensory Transduction and Cellular Signaling Cascades, W. B. Liedtke et S. Heller, Éd. Boca Raton (FL): CRC Press/Taylor & Francis, 2007</ref> | ||
TRPV1 are '''tetrameric''' channel type receptors. The four subunits from a symmetry plane around a pore allowing the passage of ions. | TRPV1 are '''tetrameric''' channel type receptors. The four subunits from a symmetry plane around a pore allowing the passage of ions. | ||
Each TRPV1 subunits are made of one '''N-terminal tail''', one '''transmembrane region''', a'' C-terminal tail'' preceded by a '''TRP domain'''. The N-terminal and C-terminal region are intracellular. N and C terminal region are responsible of 70% of the total mass of TRPV1.<ref | Each TRPV1 subunits are made of one '''N-terminal tail''', one '''transmembrane region''', a'' C-terminal tail'' preceded by a '''TRP domain'''. The N-terminal and C-terminal region are intracellular. N and C terminal region are responsible of 70% of the total mass of TRPV1.<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> | ||
The N-terminal region has 6 repeats of [https://en.wikipedia.org/wiki/Ankyrin ankyrin].<ref | The N-terminal region has 6 repeats of [https://en.wikipedia.org/wiki/Ankyrin ankyrin].<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/><ref name="Integrating TRPV1 Receptor Function with Capsaicin Psychophysics">G. Smutzer et R. K. Devassy, « Integrating TRPV1 Receptor Function with Capsaicin Psychophysics », Advances in Pharmacological Sciences, janv. 14, 2016</ref> | ||
The transmembrane region is composed of '''six transmembrane a helices''' (S1-S6). S1,S2 and S3 helices contain aromatic side chain (S1 : Y441,Y444,Y555 S2: F488 S3 : F516).<ref | The transmembrane region is composed of '''six transmembrane a helices''' (S1-S6). S1,S2 and S3 helices contain aromatic side chain (S1 : Y441,Y444,Y555 S2: F488 S3 : F516).<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> A small hydrophobic domain beetween S5 and S6 with a re-entrant loop constitutes the pore allowing the passage of ions through the TRPV1 receptor.<ref name="TRPV1"/><ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> | ||
'''Threonin''' residu (T550) and '''tyrosin''' residu (Y511) located on the fifth and the third transmembrane helices are very conserved. Threonin 550 and tyrosin 511 are implicated in TRPV1 activation by [https://en.wikipedia.org/wiki/Vanilloids vanilloids] and in pain sensation.<ref>R. Kumar, A. Hazan, A. Basu, N. Zalcman, H. Matzner, et A. Priel, « Tyrosine Residue in the TRPV1 Vanilloid Binding Pocket Regulates Deactivation Kinetics », J. Biol. Chem., vol. 291, no 26, p. 13855‑13863, juin 2016, doi: 10.1074/jbc.M116.726372.</ref> | '''Threonin''' residu (T550) and '''tyrosin''' residu (Y511) located on the fifth and the third transmembrane helices are very conserved. Threonin 550 and tyrosin 511 are implicated in TRPV1 activation by [https://en.wikipedia.org/wiki/Vanilloids vanilloids] and in pain sensation.<ref>R. Kumar, A. Hazan, A. Basu, N. Zalcman, H. Matzner, et A. Priel, « Tyrosine Residue in the TRPV1 Vanilloid Binding Pocket Regulates Deactivation Kinetics », J. Biol. Chem., vol. 291, no 26, p. 13855‑13863, juin 2016, doi: 10.1074/jbc.M116.726372.</ref> | ||
The S6 domain links the receptor to the C-terminal domain of TRPV1. The C-terminal is made of 150 amino acids and it contains '''TRP domain'''.<ref | The S6 domain links the receptor to the C-terminal domain of TRPV1. The C-terminal is made of 150 amino acids and it contains '''TRP domain'''.<ref name="Integrating TRPV1 Receptor Function with Capsaicin Psychophysics"/>.The TRP domain is made of 23-25 aminoacids with a alpha helical structure, it is found in many TRP family members.<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> TRP domain is necessary for the formation of tetrameric TRPV1. | ||
Many amino-acids of the C-terminal domain are the target of post-translationnal modifications by [https://en.wikipedia.org/wiki/Kinase kinases] and [https://en.wikipedia.org/wiki/Phosphatase phosphatases].<ref>X. Yao, H.-Y. Kwan, et Y. Huang, « Regulation of TRP Channels by Phosphorylation », Neurosignals, vol. 14, no 6, p. 273‑280, 2005, doi: 10.1159/000093042</ref> | Many amino-acids of the C-terminal domain are the target of post-translationnal modifications by [https://en.wikipedia.org/wiki/Kinase kinases] and [https://en.wikipedia.org/wiki/Phosphatase phosphatases].<ref>X. Yao, H.-Y. Kwan, et Y. Huang, « Regulation of TRP Channels by Phosphorylation », Neurosignals, vol. 14, no 6, p. 273‑280, 2005, doi: 10.1159/000093042</ref> | ||
