Journal article

A thing of beauty: Structure and function of insulin's "aromatic triplet"

Michael A Weiss, Michael C Lawrence

DIABETES OBESITY & METABOLISM | WILEY | Published : 2018

Abstract

The classical crystal structure of insulin was determined in 1969 by D.C. Hodgkin et al. following a 35-year program of research. This structure depicted a hexamer remarkable for its self-assembly as a zinc-coordinated trimer of dimer. Prominent at the dimer interface was an "aromatic triplet" of conserved residues at consecutive positions in the B chain: PheB24 , PheB25 and TyrB26 . The elegance of this interface inspired the Oxford team to poetry: "A thing of beauty is a joy forever" (John Keats as quoted by Blundell, T.L., et al. Advances in Protein Chemistry 26:279-286 [1972]). Here, we revisit this aromatic triplet in light of recent advances in the structural biology of insulin bound a..

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University of Melbourne Researchers

Grants

Awarded by Australian National Health and Medical Research Council Project Grant


Awarded by National Institutes of Health


Awarded by NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES


Funding Acknowledgements

Australian NHMRC Independent Research Institutes Infrastructure Support Scheme; Victorian State Government Operational Infrastructure Support; Australian National Health and Medical Research Council Project Grant APP1058233; Leona M. and Harry B. Helmsley Charitable Trust; JDRF; National Institutes of Health, Grant/Award Number: R01 DK040949 and DK079233; University of Chicago