reviewBiochemistryNov 30, 2006FRClosed access

Ankyrin Repeat:  A Unique Motif Mediating Protein−Protein Interactions

The Ohio State University · Institute of Biological Chemistry, Academia Sinica

PubMed
Indexed incrossrefpubmed

Abstract

Ankyrin repeat, one of the most widely existing protein motifs in nature, consists of 30-34 amino acid residues and exclusively functions to mediate protein-protein interactions, some of which are directly involved in the development of human cancer and other diseases. Each ankyrin repeat exhibits a helix-turn-helix conformation, and strings of such tandem repeats are packed in a nearly linear array to form helix-turn-helix bundles with relatively flexible loops. The global structure of an ankyrin repeat protein is mainly stabilized by intra- and inter-repeat hydrophobic and hydrogen bonding interactions. The repetitive and elongated nature of ankyrin repeat proteins provides the molecular bases of the unique…

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Authors

3

Topics & keywords

Keywords
  • Ankyrin repeat
  • Ankyrin
  • Tandem repeat
  • Protein folding
  • Protein structure
  • Biology
  • Structural motif
  • Computational biology
UN Sustainable Development Goals
  • Good health and well-being
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