人胰岛素样生长因子-1受体前三个结构域的结晶
Crystallization of the first three domains of the human insulin-like growth factor-1 receptor.
作者信息
McKern N M, Lou M, Frenkel M J, Verkuylen A, Bentley J D, Lovrecz G O, Ivancic N, Elleman T C, Garrett T P, Cosgrove L J, Ward C W
机构信息
CSIRO Division of Molecular Science, Parkville, Victoria, Australia.
出版信息
Protein Sci. 1997 Dec;6(12):2663-6. doi: 10.1002/pro.5560061223.
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).
摘要
胰岛素样生长因子-1受体（IGF-1R）是细胞增殖中至关重要的酪氨酸激酶受体。包含人IGF-1R胞外域富含半胱氨酸的L1-L2结构域的片段（第1至462位氨基酸残基）已在糖基化缺陷型Lec8细胞中过表达，并通过c-myc标签进行亲和纯化，随后进行凝胶过滤。该片段可被两种抗IGF-1R单克隆抗体24-31和24-60识别，但未显示出可检测到的与IGF-1或IGF-2的结合。IGF-1R/462在阴离子交换色谱上的等度洗脱降低了样品的异质性，从而能够产生衍射分辨率达2.6 Å的晶体，其晶胞参数为a = 77.0 Å，b = 99.5 Å，c = 120.1 Å，空间群为P2(1)2(1)2(1)。
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