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ANK Domain

No Image Several groups have solved the structure of the ANK domain from numerous different proteins including co-crystal structures of ANK domains and peptide binding partners. The ANK repeat consists of a pair of antiparallel alpha helices stacked side by side and connected by a series of intervening beta hairpin motifs. The core structure is sufficiently malleable that it can withstand a considerable degree of sequence variation at the amino acid level while maintaining a stable framework for presenting surface contact residues to mediate protein-protein interactions. The ability of ANK repeats to bind target proteins commonly involves contacts formed through the tips of the beta hairpins and the surface of the helical bundle facing the ankyrin groove. The first three N terminal ANK repeats of the yeast transcription factor Swi6 are shown.

Structure Reference: Foord, R. et al. (1999) Nat. Struc. Biol. 6(2):157-165. PDB: 1SW6. 

Domain binding and function:
Breedan and Nasmyth first reported a 33 amino acid repeat common among a small number of proteins. Subsequently, a cytoskeletal protein named Ankyrin was identified that was composed almost entirely of these short repeats. To date, ANK repeats have been identified in over 1700 different proteins from viruses, prokaryotes and eukaryotes. ANK repeats have been implicated in mediating protein-protein interactions although no common theme among the known ANK domain protein targets has been identified.
Examples of Proteins: 
ANK repeat protein
Binding partner
53BP2 (p53 binding protein) p53
p16(INK4a,d) CDK inhibitor CDK6
GABPalpha Transcription factor GABPbeta-DNA

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