Designed ankyrin repeat proteins as scaffolds for multivalent recognition |
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Authors: | Hollenbeck Jessica J Danner Derek J Landgren Rachel M Rainbolt Thomas K Roberts Danielle S |
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Institution: | Department of Chemistry, Trinity University, San Antonio, Texas 78212, United States. jessica.hollenbeck@trinity.edu |
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Abstract: | Ankyrin repeat (AR) proteins are composed of tandem repeats of a basic structural motif of ca. 33 amino acid residues that form a β-turn followed by two antiparallel α-helices. Multiple repeats stack together in a modular fashion to form a scaffold that is ideally suited for the presentation of multiple functional groups and/or recognition elements. Here we describe a biosynthetic strategy that takes advantage of the modular nature of these proteins to generate multivalent ligands that are both chemically homogeneous and structurally well-defined. Glycosylated AR proteins cluster the tetrameric lectin concanavalin A (Con A) at a rate that is comparable to the rate of Con A aggregation mediated by globular protein conjugates and variable density linear polymers. Thus, AR proteins define a new class of multivalent ligand scaffolds that have significant potential application in the study and control of a variety of multivalent interactions. |
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