Abstract
The GFRα1 cDNA was amplified by RT-PCR from fetal rat hippocampus. The soluble recombinant GFRa1 and its mutants were obtained from an Escherichia coli expression system. The biological activity of soluble GFRα1 and its mutants were evaluated in PC12 cells. The results suggest that the central domain of GFRα1 is a crucial determinant for ligand binding. This established a solid basis for further study to find the key amino acid mediating the binding of GDNF and GFRα1.
Keywords: glial cell line-derived neurotrophic factor receptor, mutation, expression, pc12 cells, surival and differentiation
Protein & Peptide Letters
Title: A Structure-Function Analysis of Glial Cell-Linederived Neurotrophic Factor Receptor Alpha1
Volume: 10 Issue: 1
Author(s): Li-Mei Wang, Zhe-Yu Chen, Qing Zhang, Wei Zhu, Da-Fu Ding, Chang-Lin Lu and Cheng He
Affiliation:
Keywords: glial cell line-derived neurotrophic factor receptor, mutation, expression, pc12 cells, surival and differentiation
Abstract: The GFRα1 cDNA was amplified by RT-PCR from fetal rat hippocampus. The soluble recombinant GFRa1 and its mutants were obtained from an Escherichia coli expression system. The biological activity of soluble GFRα1 and its mutants were evaluated in PC12 cells. The results suggest that the central domain of GFRα1 is a crucial determinant for ligand binding. This established a solid basis for further study to find the key amino acid mediating the binding of GDNF and GFRα1.
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Cite this article as:
Wang Li-Mei, Chen Zhe-Yu, Zhang Qing, Zhu Wei, Ding Da-Fu, Lu Chang-Lin and He Cheng, A Structure-Function Analysis of Glial Cell-Linederived Neurotrophic Factor Receptor Alpha1, Protein & Peptide Letters 2003; 10 (1) . https://dx.doi.org/10.2174/0929866033408318
DOI https://dx.doi.org/10.2174/0929866033408318 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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