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  • Title: Crystallization of the first three domains of the human insulin-like growth factor-1 receptor.
    Author: McKern NM, Lou M, Frenkel MJ, Verkuylen A, Bentley JD, Lovrecz GO, Ivancic N, Elleman TC, Garrett TP, Cosgrove LJ, Ward CW.
    Journal: Protein Sci; 1997 Dec; 6(12):2663-6. PubMed ID: 9416620.
    Abstract:
    The insulin-like growth factor-1 receptor (IGF-1R) is a tyrosine kinase receptor of central importance in cell proliferation. A fragment (residues 1-462) comprising the L1-cysteine rich-L2 domains of the human IGF-1R ectodomain has been overexpressed in glycosylation-deficient Lec8 cells and has been affinity-purified via a c-myc tag followed by gel filtration. The fragment was recognized by two anti-IGF-1R monoclonal antibodies, 24-31 and 24-60, but showed no detectable binding of IGF-1 or IGF-2. Isocratic elution of IGF-1R/462 on anion-exchange chromatography reduced sample heterogeneity, permitting the production of crystals that diffracted to 2.6 A resolution with cell dimensions a = 77.0 A, b = 99.5 A, c = 120.1 A, and space group P2(1)2(1)2(1).
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