Designed Ankyrin Repeat Proteins as Scaffolds for Multivalent Recognition

Citations Over Time

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.

Related Papers

• → Ankyrin Repeat: A Unique Motif Mediating Protein−Protein Interactions(2006)664 cited
• → A primer on ankyrin repeat function in TRP channels and beyond(2008)201 cited
• → The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats.(1993)108 cited
• → Alternative splicing: A key mechanism for ankyrin-B functional diversity?(2008)5 cited
• → The ANK Repeats of Erythrocyte Ankyrin Form Two Distinct but Cooperative Binding Sites for the Erythrocyte Anion Exchanger(1995)109 cited