A synthetic IgG-binding domain based on staphylococcal protein A

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ID: 306383
1987
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Abstract
A synthetic IgG-binding domain based on staphylococcal protein A was designed with the aid of sequence comparisons and computer graphic analysis. A strategy, utilizing non-palindromic restriction sites, was used to overcome the difficulties of introducing site-specific changes into the repetitive gene. A single mutagenized gene fragment was polymerized to different multiplicities, and the different gene products were expressed in Escherichia coli. Using this scheme, protein A-like proteins composed of different numbers of IgG-binding domains were produced. These domains were changed to lack asparagine--glycine dipeptide sequences as well as methionine residues and are thus, in contrast to native protein A, resistant to treatment with hydroxylamine and cyanogen bromide.
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Authors Björn Nilsson, Tomas Moks, Birger Jansson, Lars Abrahmsén, Anette Elmblad, Erik Holmgren, Christina Henrichson, Thomas A. Jones, Mathias Uhlén
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Journal Protein Engineering Design and Selection
Year 1987
DOI
10.1093/protein/1.2.107
URL
https://doi.org/10.1093/protein/1.2.107
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