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.
Reference Key
openalex_W1993870692 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Björn Nilsson, Tomas Moks, Birger Jansson, Lars Abrahmsén, Anette Elmblad, Erik Holmgren, Christina Henrichson, Thomas A. Jones, Mathias Uhlén
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
Keywords Keywords not found

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