1P4O

Structure of Apo unactivated IGF-1R KInase domain at 1.5A resolution.

Summary for 1P4O

• Entry DOI: 10.2210/pdb1p4o/pdb
• Descriptor: Insulin-like growth factor I receptor protein (2 entities in total)
• Functional Keywords: igf-1r, kinase domain, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P08069
• Total number of polymer chains: 2
• Total formula weight: 73313.92

Authors

Munshi, S.,Kornienko, M.,Hall, D.L.,Darke, P.L.,Waxman, L.,Kuo, L.C. (deposition date: 2003-04-23, release date: 2003-04-29, Last modification date: 2024-02-14)

Primary citation

Munshi, S.,Hall, D.L.,Kornienko, M.,Darke, P.L.,Kuo, L.C.
Structure of apo, unactivated insulin-like growth factor-1 receptor kinase at 1.5 A resolution.
Acta Crystallogr.,Sect.D, 59:1725-1730, 2003

PubMed Abstract: 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. Overall, the structure of the mutant IGFRK-0P is similar to that of the wild-type IGFRK-0P structure, with the exception of the previously disordered kinase-insert region in the wild type having become fixed. In addition, amino-acid residues 947-952 at the N-terminus are well defined in the mutant structure. The monomeric protein structure is folded into two lobes connected by a hinge region, with the catalytic center situated at the interface of the two lobes. Two molecules of IGFRK-0P in the asymmetric unit are associated as a dimer and two different types of dimers with their ATP-binding clefts either facing towards or away from each other are observed. The current refined model consists of a dimer and 635 water molecules.

PubMed: 14501110
DOI: 10.1107/S0907444903015415

Experimental method

X-RAY DIFFRACTION (1.5 Å)