Sandbox Reserved 1095: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 33: | Line 33: | ||
=== Ligand binding pocket === | === Ligand binding pocket === | ||
In the extracellular environment, there is a beta-hairpin in conjugation with two extracellular disulfure bridges. 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 two extracellular disulfure bridges. 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. | ||
AngII mediates AT1 receptor activation via stacking interactions between Phe8(AngII)/His256(AT1 receptor) and Tyr4(AngII)/Asn111(AT1 receptor). This phenomenon results in a conformational change in transmembrane (TM)3-TM6 helices and in interaction between TM2 and TM7. | |||
=== G protein-binding site === | === G protein-binding site === | ||