Insulin Receptor (Tyrosine Kinase Domain) Mutant with CYS 981 --> SER and TYR 984 --> PHE Mutations.
The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by
multiwavelength anomalous diffraction phasing and refined to 2.1 A resolution. The structure reveals the determinants of
substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the
tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.
 Hubbard SR; Wei L; Ellis L; Hendrickson WA (1994)
Crystal structure of the tyrosine kinase domain of
the human insulin receptor. Nature 372: 746-54. [Abstract]
 Wei L; Hubbard SR; Hendrickson WA; Ellis L (1995) Expression, characterization, and crystallization of
the catalytic core of the human insulin receptor
protein-tyrosine kinase domain.
J Biol Chem 270: 8122-30.
Not yet available
Last modified Wednesday, 30 July 1997 by Phil Bourne