Ankyrin Repeat: A Unique Motif Mediating Protein−Protein Interactions
The Ohio State University · Institute of Biological Chemistry, Academia Sinica
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…
Citation impact
- FWCI
- 7.74
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- 100%
- References
- 86
Authors
3Topics & keywords
- Ankyrin repeat
- Ankyrin
- Tandem repeat
- Protein folding
- Protein structure
- Biology
- Structural motif
- Computational biology
- Good health and well-being