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. 1997 Dec;6(12):2663–2666. doi: 10.1002/pro.5560061223

Crystallization of the first three domains of the human insulin-like growth factor-1 receptor.

N M McKern 1, M Lou 1, M J Frenkel 1, A Verkuylen 1, J D Bentley 1, G O Lovrecz 1, N Ivancic 1, T C Elleman 1, T P Garrett 1, L J Cosgrove 1, C W Ward 1
PMCID: PMC2143606  PMID: 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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Selected References

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