User:Karsten Theis/Insulin
From Proteopedia
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<scene name='82/821037/Spacfilling/1'>Mature insulin</scene> contains two chains, A and B, held together by disulfide bonds and non-covalent interactions. The surface of insulin contains quite a few hydrophobic side chains, which form protein:protein contacts when insulin forms hexamers or binds to its receptor. | <scene name='82/821037/Spacfilling/1'>Mature insulin</scene> contains two chains, A and B, held together by disulfide bonds and non-covalent interactions. The surface of insulin contains quite a few hydrophobic side chains, which form protein:protein contacts when insulin forms hexamers or binds to its receptor. | ||
| - | <jmol> | + | Sidechains colored by <jmol> |
<jmolRadioGroup> | <jmolRadioGroup> | ||
<item> | <item> | ||
<script>background white; select sidechain; color magenta; select sidechain and (cys, met, ile, leu, val, phe, tyr, trp); color gray; set echo ID bla 80% 0%; echo "hydrophobic"; color echo gray; frank off; set echo ID bla2 0% 0%; echo "hydrophilic"; color echo magenta </script> | <script>background white; select sidechain; color magenta; select sidechain and (cys, met, ile, leu, val, phe, tyr, trp); color gray; set echo ID bla 80% 0%; echo "hydrophobic"; color echo gray; frank off; set echo ID bla2 0% 0%; echo "hydrophilic"; color echo magenta </script> | ||
| - | <text> | + | <text>hydrophobiticity</text> |
<checked>true</checked> | <checked>true</checked> | ||
</item> | </item> | ||
<item> | <item> | ||
<script>select sidechain; color white; select sidechain and (asp, glu); color red; select sidechain and (lys, arg, his); color blue; set echo ID bla 80% 0%; echo "positive"; color echo blue; frank off; set echo ID bla2 0% 0%; echo "negative"; color echo red</script> | <script>select sidechain; color white; select sidechain and (asp, glu); color red; select sidechain and (lys, arg, his); color blue; set echo ID bla 80% 0%; echo "positive"; color echo blue; frank off; set echo ID bla2 0% 0%; echo "negative"; color echo red</script> | ||
| - | <text> | + | <text>charge</text> |
<checked>false</checked> | <checked>false</checked> | ||
</item> | </item> | ||
<item> | <item> | ||
| - | <script> select sidechain; | + | <script> select sidechain; color cpk; set echo ID bla 80% 0%; echo "oxygen"; color echo red; frank off; set echo ID bla2 0% 0%; echo "nitrogen"; color echo blue</script> |
| - | <text> | + | <text>element</text> |
<checked>false</checked> | <checked>false</checked> | ||
</item> | </item> | ||
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</StructureSection> | </StructureSection> | ||
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== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 15:58, 10 July 2019
Insulin is a peptide hormone that controls carbohydrate metabolism and storage in the human body[1][2]. It is secreted by specialized cells in the pancreas, enters the bloodstream and reaches other cells. There, it binds to the extracellular side of the insulin receptor, triggering tyrosine kinase activity within the target cell, which in turn regulates glucose uptake, metabolism and storage.
Contents |
Function
The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas.
Disease
Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes. It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use.
Structure
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References
- ↑ Sonksen P, Sonksen J. Insulin: understanding its action in health and disease. Br J Anaesth. 2000 Jul;85(1):69-79. PMID:10927996
- ↑ Weiss MA, Lawrence MC. A thing of beauty: Structure and function of insulin's "aromatic triplet". Diabetes Obes Metab. 2018 Sep;20 Suppl 2:51-63. doi: 10.1111/dom.13402. PMID:30230175 doi:http://dx.doi.org/10.1111/dom.13402
- ↑ Davidson HW. (Pro)Insulin processing: a historical perspective. Cell Biochem Biophys. 2004;40(3 Suppl):143-58. PMID:15289650
