Sandbox 254
From Proteopedia
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==='''Conformational Changes Beta-2 Adrenergic Receptor'''=== | ==='''Conformational Changes Beta-2 Adrenergic Receptor'''=== | ||
| - | When an agonist is in the <scene name='Sandbox_254/B2ar_morph_ser_glu_arg/ | + | When an agonist is in the <scene name='Sandbox_254/B2ar_morph_ser_glu_arg/20'>binding pocket</scene> a 2.1Å inward movement of TM5 at Ser207, highlighted in cyan, is observed. This allows for a hydrogen bond between the ligand and the receptor. This interaction appears to be a key event in activation. |
After the agonist binds, there is a rearrangement of interactions between residues located beneath the binding pocket that contributes to a rotation and outward movement of TM6. This change is associated with the breaking of the ionic lock between Glu268 in TM6 and Arg131 in TM3, resulting in an 11.4Å outward movement of the helix at the cytoplasmic face | After the agonist binds, there is a rearrangement of interactions between residues located beneath the binding pocket that contributes to a rotation and outward movement of TM6. This change is associated with the breaking of the ionic lock between Glu268 in TM6 and Arg131 in TM3, resulting in an 11.4Å outward movement of the helix at the cytoplasmic face | ||
Revision as of 01:50, 30 April 2011
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Beta-2 Adrenergic Receptor
The Beta-2 Adrenergic Receptor (B2AR) is a G-protein coupled receptor (GPCR) which, when stimulated by a catecholamine, causes the relaxation of various smooth muscles, and the production of glucose by glycogenolysis and gluconeogenesis.
Conformational Changes Beta-2 Adrenergic Receptor
When an agonist is in the a 2.1Å inward movement of TM5 at Ser207, highlighted in cyan, is observed. This allows for a hydrogen bond between the ligand and the receptor. This interaction appears to be a key event in activation.
After the agonist binds, there is a rearrangement of interactions between residues located beneath the binding pocket that contributes to a rotation and outward movement of TM6. This change is associated with the breaking of the ionic lock between Glu268 in TM6 and Arg131 in TM3, resulting in an 11.4Å outward movement of the helix at the cytoplasmic face
