Modular Control of Lectin Function: Redox-Switchable Agglutination

A specifically designed protein interface engineered into a model carbohydrate‐binding lectin (GNAP71C) generates a blood‐cell‐binding activity that can sense ambient redox conditions (see picture; DTT=dithiothreitol, GSSG=oxidized glutathione, WT=wild‐type protein, MAC=minimum agglutination concent...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2004-06, Vol.43 (23), p.3025-3029
Main Authors: McDonald, Rhona E., Hughes, David J., Davis, Benjamin G.
Format: Article
Language:English
Subjects:
Agglutination
Binding Sites
biosensors
carbohydrates
Galanthus - chemistry
lectins
Mannose-Binding Lectins - chemistry
Mannose-Binding Lectins - genetics
Mannose-Binding Lectins - metabolism
Models, Molecular
Mutation
Oxidation-Reduction
Plant Lectins - metabolism
protein engineering
receptors
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Summary:A specifically designed protein interface engineered into a model carbohydrate‐binding lectin (GNAP71C) generates a blood‐cell‐binding activity that can sense ambient redox conditions (see picture; DTT=dithiothreitol, GSSG=oxidized glutathione, WT=wild‐type protein, MAC=minimum agglutination concentration). The blood‐cell binding exploits induced extended binding that can be varied by orders of magnitude with little change in the direct carbohydrate binding.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200353320