1p4o
From Proteopedia
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Structure of Apo unactivated IGF-1R KInase domain at 1.5A resolution.
Contents |
Overview
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.
Disease
Known disease associated with this structure: Intrauterine and postnatal growth retardation OMIM:[147370]
About this Structure
1P4O is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Structure of apo, unactivated insulin-like growth factor-1 receptor kinase at 1.5 A resolution., Munshi S, Hall DL, Kornienko M, Darke PL, Kuo LC, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1725-30. Epub 2003, Sep 19. PMID:14501110
Page seeded by OCA on Thu Feb 21 14:25:03 2008
