| Autor: |
Mckern, Neil M., Frenkel, Maurice J., Verkuylen, Amanda, Bentley, John D., Lovrecz, George O., Ivancic, Neva, Elleman, Thomas C., Cosgrove, Leah J., Lou, Meizhen, Garrett, THOMAS P. J., Ward, Colin W. |
| Zdroj: |
Protein Science: A Publication of the Protein Society; 1997, Vol. 6 Issue 12, p2663-2666, 4p |
| Abstrakt: |
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 Å resolution with cell dimensions a = 77.0 A, Å = 99.5 Å, c = 120.1 Å, and space group P212121. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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