Aromatic Anchor at an Invariant Hormone-Receptor Interface: FUNCTION OF INSULIN RESIDUE B24 WITH APPLICATION TO PROTEIN DESIGN

Crystallographic studies of insulin bound to fragments of the insulin receptor have recently defined the topography of the primary hormone-receptor interface. Here, we have investigated the role of Phe(B24), an invariant aromatic anchor at this interface and site of a human mutation causing diabetes...

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Bibliographic Details
Published in:J Biol Chem
Main Authors: Pandyarajan, Vijay, Smith, Brian J., Phillips, Nelson B., Whittaker, Linda, Cox, Gabriella P., Wickramasinghe, Nalinda, Menting, John G., Wan, Zhu-li, Whittaker, Jonathan, Ismail-Beigi, Faramarz, Lawrence, Michael C., Weiss, Michael A.
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2014
Subjects:
Protein Structure and Folding
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC4263875/
https://ncbi.nlm.nih.gov/pubmed/25305014
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M114.608562
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