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

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: Phe^B24 , Phe^B25 and Tyr^B26 . 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 as a monomer to fragments of the insulin receptor. Such co-crystal s

SUBMITTER: Weiss MA 

PROVIDER: S-EPMC6159917 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature