Andrew Helmerich Sandbox 1: Difference between revisions
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It is hypothesized that amylin binds to the receptor via a two-domain model (Figure 2). 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. Once both the c-terminus and n-terminus of amylin are bound, the receptor becomes activated. [[Image:Domain_drawingnew.jpg|300px|left|thumb|Figure 2: The Two Domain Model]] | It is hypothesized that amylin binds to the receptor via a two-domain model (Figure 2). 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. Once both the c-terminus and n-terminus of amylin are bound, the receptor becomes activated. [[Image:Domain_drawingnew.jpg|300px|left|thumb|Figure 2: The Two Domain Model]] | ||
====RAMP-CTR Interface==== | ====RAMP-CTR Interface==== | ||
<scene name='10/1038828/Ramp_ctr_interface/ | <scene name='10/1038828/Ramp_ctr_interface/10'>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 ==== | ||
The extracellular domain of the CTR primarily contains polar residues in the extracellular space. In order to orient these residues to facilitate amylin binding, <scene name='10/1038828/Ctr_ramp_ecd_stablization/8'>RAMP makes hydrogen bonds with the CTR</scene> to increase the rigidity of the receptor binding site. | The extracellular domain of the CTR primarily contains polar residues in the extracellular space. In order to orient these residues to facilitate amylin binding, <scene name='10/1038828/Ctr_ramp_ecd_stablization/8'>RAMP makes hydrogen bonds with the CTR</scene> to increase the rigidity of the receptor binding site. | ||
