1IRK

Insulin Receptor (Tyrosine Kinase Domain) Mutant with CYS 981 --> SER and TYR 984 --> PHE Mutations.



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Synopsis

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.

References

[1] 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]

[2] 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.

Walk Through

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Sequence Information


Last modified Wednesday, 30 July 1997 by Phil Bourne