Designed ankyrin repeat proteins as scaffolds for multivalent recognition.
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.
Department of Chemistry, Trinity University, San Antonio, Texas 78212, United States. jessica.hollenbeck@trinity.edu
Jessica J
JJ
Hollenbeck
Derek J
DJ
Danner
Rachel M
RM
Landgren
Thomas K
TK
Rainbolt
Danielle S
DS
Roberts
D017089:Ankyrin Repeat; D017487:Ankyrins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D003208:Concanavalin A / Q000737:chemistry; D004926:Escherichia coli; D006031:Glycosylation; D008958:Models, Molecular; D010316:Particle Size; D011485:Protein Binding; D015202:Protein Engineering; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
D017487:Ankyrins; D011994:Recombinant Proteins; D003208:Concanavalin A