Insulin Structure & Function

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==Structure==
==Structure==
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Insulin is composed of two different types of peptide chains. <scene name='34/347648/Chain_a/1'>Chain A</scene> has 21 amino acids and <scene name='34/347648/Chain_b/1'>Chain B</scene> has 30 amino acids. Both chains contain <scene name='34/347648/Secondary_structures/1'>alpha helices</scene> but no beta strands. There are 3 conserved <scene name='34/347648/Disulfide_bonds/1'>disulfide bridges</scene> which help keep the two chains together. Insulin can also form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_dimer/2'>dimers</scene> in solution due to the hydrogen bonding between the B chains (shown as white lines). The dimers can further interact to form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_hexamer/4'>hexamers</scene> due to interaction between hydrophobic surfaces. This <scene name='User:Whitney_Stoppel/sandbox1/Insulin_ph7/2'>scene highlights</scene> the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7. Indeed "fast acting" insulin is produced by switching the last two amino acids, which reduces the formation of the hexameric insulin.
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Insulin is composed of two different types of peptide chains. <scene name='34/347648/Chain_a/1'>Chain A</scene> has 21 amino acids and <scene name='34/347648/Chain_b/1'>Chain B</scene> has 30 amino acids. Both chains contain <scene name='34/347648/Secondary_structures/1'>alpha helices</scene> but no beta strands. There are 3 conserved <scene name='34/347648/Disulfide_bonds/1'>disulfide bridges</scene> which help keep the two chains together. Insulin can also form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_dimer/2'>dimers</scene> in solution due to the hydrogen bonding between the B chains (shown as white lines). The dimers can further interact to form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_hexamer/4'>hexamers</scene> due to interaction between hydrophobic surfaces. This <scene name='User:Whitney_Stoppel/sandbox1/Insulin_ph7/2'>scene highlights</scene> the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.
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A number of insulin variants have been made to favor either the monomeric or hexameric form. Deletion of the <scene name='34/347648/Hexamer_bchaincterminus/2'>five C terminal residues of the B chain</scene> creates a monomer only form. This portion of the B chain is involved in <scene name='34/347648/Dimer_bchainctermhbond/1'>hydrogen bonds</scene> between the B chain of one monomer and the A (marked C) and B (marked D) chain of another monomer.
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</StructureSection>
</StructureSection>
==3D structures of insulin==
==3D structures of insulin==

Revision as of 22:03, 15 June 2015

Human insulin chain A (grey) and chain B (green), 2hiu

Drag the structure with the mouse to rotate

3D structures of insulin

Insulin

Additional Resources

Thanks to 'User:Whitney_Stoppel' for the hexameric insulin scenes. For additional information, see: Diabetes & Hypoglycemia

Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Michal Harel, David Canner, Pat McQuaid

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