1qiy
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HUMAN INSULIN HEXAMERS WITH CHAIN B HIS MUTATED TO TYR COMPLEXED WITH PHENOL
OverviewOverview
The addition of phenols to hexameric insulin solutions produces a, particularly stable hexamer, resulting from a rearrangement in which, residues B1-B8 change from an extended conformation (T-state) to form an, alpha-helix (R-state). The R-state is, in part, stabilized by nonpolar, interactions between the phenolic molecule and residue B5 His at the, dimer-dimer interface. The B5 His --> Tyr mutant human insulin was, constructed to see if the tyrosine side chain would mimic the effect of, phenol binding in the hexamer and induce the R-state. In partial support, of this hypothesis, the molecule crystallized as a half-helical hexamer, (T(3)R(3)) in conditions that conventionally promote the fully nonhelical, (T6) form. As expected, in the presence of phenol or resorcinol, the B5, Tyr ... [(full description)]
About this StructureAbout this Structure
1QIY is a [Protein complex] structure of sequences from [Homo sapiens] with ZN, CL and IPH as [ligands]. Structure known Active Sites: ZN1 and ZN2. Full crystallographic information is available from [OCA].
ReferenceReference
Structural consequences of the B5 histidine --> tyrosine mutation in human insulin characterized by X-ray crystallography and conformational analysis., Tang L, Whittingham JL, Verma CS, Caves LS, Dodson GG, Biochemistry. 1999 Sep 14;38(37):12041-51. PMID:10508408
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