GLP-1: Difference between revisions
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Glucagon-like peptide 1 (GLP-1) is a hormone involved in insulin regulation. It was discovered when researchers found that glucose in the digestive tract led to higher insulin levels than the same amount of glucose administered directly in the blood stream<ref>PMID: 31767182</ref>. GLP-1 is produced in specialized cells in the intestine and in the pancreas, is released into the blood and has effects on cells in the pancreas, in the brain, and in many other organs. The half-life of GLP-1 is on the order of minutes, so it exerts a short-term effect unless continuously produced. | Glucagon-like peptide 1 (GLP-1) is a hormone involved in insulin regulation. It was discovered when researchers found that glucose in the digestive tract led to higher insulin levels than the same amount of glucose administered directly in the blood stream<ref>PMID: 31767182</ref>. GLP-1 is produced in specialized cells in the intestine and in the pancreas, is released into the blood and has effects on cells in the pancreas, in the brain, and in many other organs. The half-life of GLP-1 is on the order of minutes, so it exerts a short-term effect unless continuously produced. | ||
<StructureSection size='340' side='right' scene=' | <StructureSection size='340' side='right' scene='10/1067195/Crystal/1'> | ||
== Structure == | == Structure == | ||
Bound to the GLP-1 receptor, GLP-1 has an <scene name='10/1067195/Glp1_only/1'>alpha-helical structure</scene> that is <scene name='10/1067195/Cv1/1'>bent</scene> near glycine in some complexes. In solution, GLP-1 is <scene name='10/1067195/Glp-1_solution/1'>alpha-helical in its center</scene> according to NMR data when in the presence of helix-stabilizers, and fairly unstructured otherwise<ref>DOI:10.1002/mrc.880</ref>. Looking at the helix-propensity of the peptide sequence, the N-terminal part of Glp-1 (7-37) is less likely to be alpha-helical than the C-terminal half. | Bound to the GLP-1 receptor, GLP-1 has an <scene name='10/1067195/Glp1_only/1'>alpha-helical structure</scene> that is <scene name='10/1067195/Cv1/1'>bent</scene> near glycine in some complexes. In solution, GLP-1 is <scene name='10/1067195/Glp-1_solution/1'>alpha-helical in its center</scene> according to NMR data when in the presence of helix-stabilizers, and fairly unstructured otherwise<ref>DOI:10.1002/mrc.880</ref>. Looking at the helix-propensity of the peptide sequence, the N-terminal part of Glp-1 (7-37) is less likely to be alpha-helical than the C-terminal half. | ||
