Sandbox Ben Whiteside: Difference between revisions

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=== Two-Domain Model of Amylin Binding ===
=== Two-Domain Model of Amylin Binding ===
It is hypothesized that amylin binds to the receptor via a two-domain model. The model suggests a series of steps for how amylin binds. First, the c-terminus of amylin binds to the n terminus of the extracellular domain of the receptor. This binding factors the alignment of amylin's n-terminus to the primary GPCR binding site. This activates the GPCR, leading to subsequent activation of adenylyl cyclase and cAMP release. [[Image:Domain_drawingnew.jpg|300px|left|thumb|Two Domain Model ]]
It is hypothesized that amylin binds to the receptor via a two-domain model. The model suggests a series of steps for how amylin binds. First, the c-terminus of amylin binds to the n terminus of the extracellular domain of the receptor. This binding factors the alignment of amylin's n-terminus to the primary GPCR binding site. This activates the GPCR, leading to subsequent activation of adenylyl cyclase and cAMP release. [[Image:Domain_drawingnew.jpg|300px|left|thumb|Two Domain Model ]]
===RAMP-CTR Interface
===RAMP-CTR Interface===
<scene name='10/1038828/Ramp_ctr_interface/9'>RAMP CTR Interface </scene> is a key interaction that stabilizes the protein complex and positions the receptor to favorably bind to amylin. The RAMP-CTR interface extends into the plasma membrane, providing additional non-covalent bonding between the protein complex and the cell membrane.  
<scene name='10/1038828/Ramp_ctr_interface/9'>RAMP CTR Interface </scene> is a key interaction that stabilizes the protein complex and positions the receptor to favorably bind to amylin. The RAMP-CTR interface extends into the plasma membrane, providing additional non-covalent bonding between the protein complex and the cell membrane.  
==== Extracellular Domain - RAMP interactions ====
==== Extracellular Domain - RAMP interactions ====