Sandbox Reserved 1095: Difference between revisions

Line 32:

=== Ligand binding pocket ===

In the extracellular environment, there is a beta-hairpin in conjugation with <scene name='82/829348/Disulfuric_bridge/1'>two extracellular disulfure bridges</scene>. This structure is responsible for the opening and the locking of the ligand binding pocket <ref ~~name="Fillion2013"~~> ~~[https~~://www.ncbi.nlm.nih.gov/pmc/articles/PMC3605637/ Fillion D, Cabana J, Guillemette G, Leduc R, Lavigne P, Escher E. Structure of the human angiotensin II type 1 (AT1) receptor bound to angiotensin II from multiple chemoselective photoprobe contacts reveals a unique peptide binding mode. J Biol Chem. 2013;288(12):8187–8197. doi:10.1074/jbc.M112.442053] </ref>. The ligand goes into an <scene name='82/829348/Ligand_blinding_pocket/1'>hydrophilic pocket</scene> created into the membrane thanks to the 7 alpha helix which create a gate between the membrane and the extracellular environment.

In the extracellular environment, there is a beta-hairpin in conjugation with <scene name='82/829348/Disulfuric_bridge/1'>two extracellular disulfure bridges</scene>. This structure is responsible for the opening and the locking of the ligand binding pocket <ref> PMID: 23386604 </ref>. The ligand goes into an <scene name='82/829348/Ligand_blinding_pocket/1'>hydrophilic pocket</scene> created into the membrane thanks to the 7 alpha helix which create a gate between the membrane and the extracellular environment.

AngII mediates AT1 receptor activation via stacking interactions between Phe8(AngII)/<scene name='82/829348/His_256/1'>His256</scene>(AT1 receptor) and Tyr4(AngII)/<scene name='82/829348/Asn_111/1'>Asn111</scene>(AT1 receptor). This phenomenon results in a conformational change in transmembrane (TM)3-TM6 helices and in interaction between TM2 and TM7.

Sandbox Reserved 1095: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 32: / Line 32: @@
 === Ligand binding pocket ===
-In the extracellular environment, there is a beta-hairpin in conjugation with <scene name='82/829348/Disulfuric_bridge/1'>two extracellular disulfure bridges</scene>. This structure is responsible for the opening and the locking of the ligand binding pocket <ref name="Fillion2013"> [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3605637/ Fillion D, Cabana J, Guillemette G, Leduc R, Lavigne P, Escher E. Structure of the human angiotensin II type 1 (AT1) receptor bound to angiotensin II from multiple chemoselective photoprobe contacts reveals a unique peptide binding mode. J Biol Chem. 2013;288(12):8187–8197. doi:10.1074/jbc.M112.442053] </ref>. The ligand goes into an <scene name='82/829348/Ligand_blinding_pocket/1'>hydrophilic pocket</scene> created into the membrane thanks to the 7 alpha helix which create a gate between the membrane and the extracellular environment.
+In the extracellular environment, there is a beta-hairpin in conjugation with <scene name='82/829348/Disulfuric_bridge/1'>two extracellular disulfure bridges</scene>. This structure is responsible for the opening and the locking of the ligand binding pocket <ref> PMID: 23386604  </ref>. The ligand goes into an <scene name='82/829348/Ligand_blinding_pocket/1'>hydrophilic pocket</scene> created into the membrane thanks to the 7 alpha helix which create a gate between the membrane and the extracellular environment.
 AngII mediates AT1 receptor activation via stacking interactions between Phe8(AngII)/<scene name='82/829348/His_256/1'>His256</scene>(AT1 receptor) and Tyr4(AngII)/<scene name='82/829348/Asn_111/1'>Asn111</scene>(AT1 receptor). This phenomenon results in a conformational change in transmembrane (TM)3-TM6 helices and in interaction between TM2 and TM7.