Insulin Structure & Function

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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.
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; without this region, the hexamers do not form. Lispro is another fast acting insulin; it has the lysine and proline at the end of the B subunit swapped. This allows the lysine to make a <scene name='34/347648/Lispro_h_bonds/1'>hydrogen bond</scene> with tyrosine 26 and his 5 of the same chain, which also favors formation of the active monomer state.
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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; without this region, the hexamers do not form. Lispro is another fast acting insulin; it has the lysine and proline at the end of the B subunit swapped. This allows the lysine to make a <scene name='34/347648/Lispro_h_bonds/2'>hydrogen bond</scene> with tyrosine 26, which also favors formation of the active monomer state.
</StructureSection>
</StructureSection>

Current revision

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

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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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