Human insulin analogues modified at the B26 site reveal a hormone conformation that is undetected in the receptor complex

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 natur...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2014-10, Vol.70 (10), p.2765-2774
Hauptverfasser:	Žáková, Lenka, Kletvíková, Emília, Lepšík, Martin, Collinsová, Michaela, Watson, Christopher J., Turkenburg, Johan P., Jiráček, Jiří, Brzozowski, Andrzej M.
Format:	Artikel
Sprache:	eng
Schlagworte:	active conformation Amino Acid Substitution Animals Cells, Cultured complex COMPLEXES CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY Crystallography, X-Ray Fibroblasts - metabolism Humans Hyperglycemia Insulin Insulin - analogs & derivatives Insulin - chemistry Insulin - genetics Insulin - metabolism insulin receptor INTERACTIONS INTERFACES isothermal titration microcalorimetry Lymphocytes - metabolism Male Mice Mice, Knockout Models, Molecular MODIFICATIONS molecular dynamics MOLECULAR DYNAMICS METHOD Mutation ORIGIN Phenylalanine Protein Conformation Rats, Wistar Receptor, Insulin - chemistry Receptor, Insulin - metabolism RECEPTORS Research Papers SPECIFICITY SPECTRA
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