Glucagon-like peptide 1 receptor: Difference between revisions

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The 3D structure of the complex of GLP-1R and GLP-1 shows the GLP-1 peptide as a kinked helix. The ampiphilic GLP-1 helix shows <scene name='84/841095/Cv/2'>hydrophilic</scene> and <scene name='84/841095/Cv/3'>hydrophobic</scene> interactions with GLP-1R on opposite faces<ref>PMID:19861722</ref>. <scene name='84/841095/Cv/5'>GLP-1R/GLP-1 salt bridges and H-bonds</scene>.
The 3D structure of the complex of GLP-1R and GLP-1 shows the GLP-1 peptide as a kinked helix. The ampiphilic GLP-1 helix shows <scene name='84/841095/Cv/2'>hydrophilic</scene> and <scene name='84/841095/Cv/3'>hydrophobic</scene> interactions with GLP-1R on opposite faces<ref>PMID:19861722</ref>. <scene name='84/841095/Cv/5'>GLP-1R/GLP-1 salt bridges and H-bonds</scene>.
See also:
* [[G protein-coupled receptor]]
*[[Receptor]]
*[[Transmembrane (cell surface) receptors]]
</StructureSection>
</StructureSection>


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Michal Harel, Alexander Berchansky, Karsten Theis