Contribution of Tyr(B26) to the Function and Stability of Insulin: STRUCTURE-ACTIVITY RELATIONSHIPS AT A CONSERVED HORMONE-RECEPTOR INTERFACE

Crystallographic studies of insulin bound to receptor domains have defined the primary hormone-receptor interface. We investigated the role of Tyr(B26), a conserved aromatic residue at this interface. To probe the evolutionary basis for such conservation, we constructed 18 variants at B26. Surprisin...

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Bibliografiset tiedot
Julkaisussa:J Biol Chem
Päätekijät: Pandyarajan, Vijay, Phillips, Nelson B., Rege, Nischay, Lawrence, Michael C., Whittaker, Jonathan, Weiss, Michael A.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Society for Biochemistry and Molecular Biology 2016
Aiheet:
Protein Structure and Folding
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC4933216/
https://ncbi.nlm.nih.gov/pubmed/27129279
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M115.708347
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