Sandbox Reserved 1652: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Chloe Reynas (talk | contribs) No edit summary |
Chloe Reynas (talk | contribs) No edit summary |
||
| Line 20: | Line 20: | ||
'''Threonin''' residue (<scene name='86/868185/T550/1'>T550</scene>) and '''Tyrosin''' residue (<scene name='86/868185/Y511/2'>Y511</scene>) located on the fifth and the third transmembrane helices are very conserved. Threonin 550 and Aspargin 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''' residue (<scene name='86/868185/T550/1'>T550</scene>) and '''Tyrosin''' residue (<scene name='86/868185/Y511/2'>Y511</scene>) located on the fifth and the third transmembrane helices are very conserved. Threonin 550 and Aspargin 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 '''<scene name='86/868185/Trp/1'>TRP domain</scene>'''.<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. | The S6 domain links the receptor to the <scene name='86/868185/C_term/1'>C-terminal</scene> domain of TRPV1. The C-terminal is made of 150 amino acids and it contains '''<scene name='86/868185/Trp/1'>TRP domain</scene>'''.<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> | ||
