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

Protein Science : a Publication of the Protein Society
N M McKernC W Ward

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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Citations

Aug 9, 2006·Proceedings of the National Academy of Sciences of the United States of America·Meizhen LouColin W Ward
Jan 21, 2012·Protein Expression and Purification·Natalia DavydovaMarc G Achen
Jul 31, 2007·The International Journal of Biochemistry & Cell Biology·Sarawut JitrapakdeeJohn C Wallace
Oct 26, 2018·Nature Communications·Felix WeisMichael C Lawrence
Nov 27, 1999·The Journal of Biological Chemistry·C N WoldinG G Shipley
Jun 10, 2016·The Journal of Biological Chemistry·Callum F LawrenceMichael C Lawrence
May 28, 2020·Structure·Yibin XuMichael C Lawrence

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