Structure of apo, unactivated insulin-like growth factor-1 receptor kinase at 1.5 A resolution.

@article{Munshi2003StructureOA,
  title={Structure of apo, unactivated insulin-like growth factor-1 receptor kinase at 1.5 A resolution.},
  author={Sanjeev K Munshi and Dawn L Hall and Maria Kornienko and Paul L. Darke and Lawrence C Kuo},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2003},
  volume={59 Pt 10},
  pages={1725-30}
}
The crystal structure of the wild-type unactivated kinase domain (IGFRK-0P) of insulin-like growth factor-1 receptor has been reported previously at 2.7 A resolution [Munshi et al. (2002), J. Biol. Chem. 277, 38797-38802]. In order to obtain a high-resolution structure, a number of variants of IGFRK-0P were prepared and screened for crystallization. A double mutant with E1067A and E1069A substitutions within the kinase-insert region resulted in crystals that diffracted to 1.5 A resolution… CONTINUE READING