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Ligand binding by repeat proteins: natural and designed.


ABSTRACT: Repeat proteins contain tandem arrays of small structural motifs. As a consequence of this architecture, they adopt non-globular, extended structures that present large, highly specific surfaces for ligand binding. Here we discuss recent advances toward understanding the functional role of this unique modular architecture. We showcase specific examples of natural repeat proteins interacting with diverse ligands and also present examples of designed repeat protein-ligand interactions.

SUBMITTER: Grove TZ 

PROVIDER: S-EPMC3500881 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

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Ligand binding by repeat proteins: natural and designed.

Grove Tijana Z TZ   Cortajarena Aitziber L AL   Regan Lynne L  

Current opinion in structural biology 20080723 4


Repeat proteins contain tandem arrays of small structural motifs. As a consequence of this architecture, they adopt non-globular, extended structures that present large, highly specific surfaces for ligand binding. Here we discuss recent advances toward understanding the functional role of this unique modular architecture. We showcase specific examples of natural repeat proteins interacting with diverse ligands and also present examples of designed repeat protein-ligand interactions. ...[more]

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