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A Structure-Function Analysis of Glial Cell-Linederived Neurotrophic Factor Receptor Alpha1

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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: expression; glial cell line-derived neurotrophic factor recept; mutation; pc12 cells; surival and differentiation

Document Type: Review Article


Publication date: 2003-02-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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