Semaglutide: Difference between revisions
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[[Image:GLP-1 semaglutide.png|700px]] | [[Image:GLP-1 semaglutide.png|700px]] | ||
Bound to the GLP-1 receptor, the peptide forms a single <scene name='10/1062575/Semaglutide/1'>alpha helix</scene>, just like <scene name='10/1067195/Glp1_only/1'>GLP-1</scene>. Semaglutide interacts with the transmembrane and the extracellular portions of the <scene name='10/1062575/Semaglutide_and_receptor/1'>receptor</scene><ref>PMID: 34260945</ref><ref name="discovery"/>. Interactions of the <scene name='10/1062575/Semaglutide_and_receptor/4'>C-terminal part of semaglutide with the extracellular domain</scene> include a hydrophobic patch (), an ionic interaction (), and hydrogen bonds (). Interactions of the <scene name='10/1062575/Semaglutide_and_receptor/5'>N-terminal domain of semaglutide with the transmembrane helices</scene> are extensive, including () and (). | Bound to the GLP-1 receptor, the peptide forms a single <scene name='10/1062575/Semaglutide/1'>alpha helix</scene>, just like <scene name='10/1067195/Glp1_only/1'>GLP-1</scene>. | ||
Semaglutide interacts with the transmembrane and the extracellular portions of the <scene name='10/1062575/Semaglutide_and_receptor/1'>receptor</scene><ref>PMID: 34260945</ref><ref name="discovery"/>. The N-terminal residues (<jmol> | |||
<jmolLink> | |||
<script> | |||
define current selected; | |||
select 7-20 and :P; | |||
selectionHalos on; | |||
delay 0.5; | |||
selectionHalos off; | |||
select current; | |||
</script> | |||
<text>☼</text> | |||
</jmolLink> | |||
</jmol>) of the peptide agonist binds deeply into the transmembrane portion while the C-terminal residues (<jmol> | |||
<jmolLink> | |||
<script> | |||
define current selected; | |||
select 27-37 and :P; | |||
selectionHalos on; | |||
delay 0.5; | |||
selectionHalos off; | |||
select current; | |||
</script> | |||
<text>☼</text> | |||
</jmolLink> | |||
</jmol>) interact with the extracellular domain. Lysine 26 (<jmol> | |||
<jmolLink> | |||
<script> | |||
define current selected; | |||
select 26:P; | |||
selectionHalos on; | |||
delay 0.5; | |||
selectionHalos off; | |||
select current; | |||
</script> | |||
<text>☼</text> | |||
</jmolLink> | |||
</jmol>) is located in a solvent-exposed area, allowing the fatty acid and linker (<jmol> | |||
<jmolLink> | |||
<script> | |||
define current selected; | |||
select 26:P; | |||
selectionHalos on; | |||
delay 0.5; | |||
selectionHalos off; | |||
select current; | |||
</script> | |||
<text>☼</text> | |||
</jmolLink> | |||
</jmol>) to be attached without interfering with receptor binding. | |||
Interactions of the <scene name='10/1062575/Semaglutide_and_receptor/4'>C-terminal part of semaglutide with the extracellular domain</scene> include a hydrophobic patch (), an ionic interaction (), and hydrogen bonds (). Interactions of the <scene name='10/1062575/Semaglutide_and_receptor/5'>N-terminal domain of semaglutide with the transmembrane helices</scene> are extensive, including () and (). | |||
==Half-life== | ==Half-life== | ||
