Article
Aromatic anchor at an invariant hormone-receptor interface: function of insulin residue B24 with application to protein design.
The Journal of biological chemistry - 12 Dec 2014
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
Abstract excerpt
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 mellitus. An extensive set of B24 substitutions has been constructed and tested for effects on receptor binding....
Topics
- Amino Acid Sequence
- Animals
- Conserved Sequence
- Drug Design
- Humans
- Hydrophobic and Hydrophilic Interactions
- Insulin
- Kinetics
- Models, Molecular
- Molecular Sequence Data