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• W2089103294 abstract "The cohesin-dockerin interaction provides the basis for incorporation of the individual enzymatic subunits into the cellulosome complex. In a previous article (Pagés et al., Proteins 1997;29:517-527) we predicted that four amino acid residues of the approximately 70-residue dockerin domain would serve as recognition codes for binding to the cohesin domain. The validity of the prediction was examined by site-directed mutagenesis of the suspected residues, whereby the species-specificity of the cohesin-dockerin interaction was altered. The results support the premise that the four residues indeed play a role in biorecognition, while additional residues may also contribute to the specificity of the interaction. Proteins 2000;39:170-177." @default.
• W2089103294 created "2016-06-24" @default.
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• W2089103294 date "2000-05-01" @default.
• W2089103294 modified "2023-10-18" @default.
• W2089103294 title "Cohesin-dockerin recognition in cellulosome assembly: Experiment versus hypothesis" @default.
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• W2089103294 doi "https://doi.org/10.1002/(sici)1097-0134(20000501)39:2<170::aid-prot7>3.0.co;2-h" @default.
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