Sandbox Reserved 1652: Difference between revisions
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The N-terminal region has 6 repeats of [https://en.wikipedia.org/wiki/Ankyrin <scene name='86/868185/Ankyrin_residues_of_n-term/1'>ankyrin</scene>].<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 N-terminal region has 6 repeats of [https://en.wikipedia.org/wiki/Ankyrin <scene name='86/868185/Ankyrin_residues_of_n-term/1'>ankyrin</scene>].<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''' (<scene name='86/868185/S1/1'>S1</scene>,<scene name='86/868185/S2/1'>S2</scene>,<scene name='86/868185/S3/1'>S3</scene>,<scene name='86/868185/S4/1'>S4</scene>,<scene name='86/868185/S5/1'>S5</scene>,S6). S1,S2 and S3 helices contain aromatic side chain (<scene name='86/868185/Aromatic_residues_of_s1_s2_s3/1'>S1 : Y441,Y444,Y555 S2: F488 S3 : F516</scene>).<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> A small hydrophobic domain beetween S5 and S6 with a <scene name='86/868185/Re_entrant_loop/1'>re-entrant loop</scene> 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"/> | The transmembrane region is composed of '''six transmembrane a helices''' (<scene name='86/868185/S1/1'>S1</scene>,<scene name='86/868185/S2/1'>S2</scene>,<scene name='86/868185/S3/1'>S3</scene>,<scene name='86/868185/S4/1'>S4</scene>,<scene name='86/868185/S5/1'>S5</scene>,<scene name='86/868185/S6/1'>S6</scene>). S1,S2 and S3 helices contain aromatic side chain (<scene name='86/868185/Aromatic_residues_of_s1_s2_s3/1'>S1 : Y441,Y444,Y555 S2: F488 S3 : F516</scene>).<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> A small hydrophobic domain beetween S5 and S6 with a <scene name='86/868185/Re_entrant_loop/1'>re-entrant loop</scene> 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 (<scene name='86/868185/T550/1'>T550</scene>) and '''Tyrosin''' reside (<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''' residu (<scene name='86/868185/T550/1'>T550</scene>) and '''Tyrosin''' reside (<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> | ||
