|PROSITE documentation PDOC50088|
Ankyrin repeats (ANK) are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers .
Many ankyrin repeat regions are known to function as protein-protein interaction domains.
The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures, e.g. from:
It has been described as an L-shaped structure consisting of a β-hairpin and two α-helices .
Two profiles were developed for this module, the first one picks up ANK repeats while the second profile is 'circular' and will thus detect a region containing adjacent ANK repeats.Last update:
December 2001 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
|Title||Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?|
|2||Authors||Gorina S. Pavletich N.P.|
|Title||Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2.|
|3||Authors||Luh F.Y. Archer S.J. Domaille P.J. Smith B.O. Owen D. Brotherton D.H. Raine A.R. Xu X. Brizuela L. Brenner S.L. Laue E.D.|
|Title||Structure of the cyclin-dependent kinase inhibitor p19Ink4d.|
|4||Authors||Batchelor A.H. Piper D.E. de la Brousse F.C. McKnight S.L. Wolberger C.|
|Title||The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA.|
|5||Authors||Jacobs M.D. Harrison S.C.|
|Title||Structure of an IkappaBalpha/NF-kappaB complex.|