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Insulin Structure

Conserved histidine in insulin is required for foldability of human proinsulin

Published in Obesity and Diabetes Week, October 16th, 2006

A conserved histidine in insulin is required for the foldability of human proinsulin.

"The insulins of eutherian mammals contain histidines at positions B5 and B10. The role of HisB10 is well defined: although not required in the mature hormone for receptor binding, in the islet beta cell this side chain functions in targeting proinsulin to glucose-regulated secretory granules and provides axial zinc-binding sites in storage hexamers. In contrast, the role of HisB5 is less well understood," scientists in the United States report.

"Here," recount Q.X. Hua and colleagues, University of Michigan, "we demonstrate that its...

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