Article
Human insulin analogues modified at the B26 site reveal a hormone conformation that is undetected in the receptor complex.
Acta crystallographica. Section D, Biological crystallography - 1 Oct 2014
Záková Lenka, Kletvíková Emília, Lepšík Martin, Collinsová Michaela, Watson Christopher J, Turkenburg Johan P, Jiráček Jiří, Brzozowski Andrzej M
Abstract excerpt
The structural characterization of the insulin-insulin receptor (IR) interaction still lacks the conformation of the crucial B21-B30 insulin region, which must be different from that in its storage forms to ensure effective receptor binding. Here, it is shown that insulin analogues modified by natural amino acids at the TyrB26 site can represent an active form of this hormone. In particular, [AsnB26]-insulin and...
Topics
- Amino Acid Substitution
- Animals
- Cells, Cultured
- Crystallography, X-Ray
- Fibroblasts
- Humans
- Insulin
- Lymphocytes
- Male
- Mice
- Mice, Knockout
- Models, Molecular
- Mutation