Ankyrin Repeat

The ankyrin repeat motif is one of the most common protein-protein interaction domains. Ankyrin repeats are modules of about 33 amino acids repeated in tandem. They are found in a large number of proteins with diverse cellular functions such as transcriptional regulators, signal transducers, cell-cycle regulators, and cytoskeletal proteins. 

Axton JM, Shamanski FL, Young LM, Henderson DS, Boyd JB, Orr-Weaver TL 1994 The inhibitor of DNA replication encoded by the Drosophila gene plutonium is a small, ankyrin repeat protein. EMBO J 13 462-470... 

The specific domains that recognize KMe have been described within several protein families the so-called "royal family" of Tudor, Agenet, chromo, PWWP, and MBT domains the plant homeodomain (PHD) the WD40 repeat protein—WDR5 and ankyrin repeats [37,38]. Given the rapid rate of progress in this area, the relatively low affinity of these interactions (Kd values typically 10-100 jjM), the wide variety of... 

Kamuea, T., et al.. The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families. Genes Dev,... 

I/cBa substrate peptide (Figure 7.11). These isolated j5-catenin and I/cBa peptides should accurately reflect the context of these destruction motifs in their respective full-length proteins, since Lysl9 and the destruction motif of j5-catenin are both in a 133-residue N-terminal region that has been previously shown to have a disordered structure by proteolytic digestion analysis [104]. The destruction motif of I/cBa similarly resides outside the structured ankyrin-repeat domain. 

Cohen, S., Orian, A., and Ciechanover, A. (2001). Processing of pl05 is inhibited by docking of p50 active subunits to the ankyrin repeat domain, and inhibition is alleviated by signaling via the C-terminal phosphorylation/ ubiquitin-ligase binding domain. J. Biol. Chem. 276, 26769-76. 

Jin, X., Touhey J. and Caudet, R. (2006). Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J. Biol. Chem. 281,25006-25010. 

Kohl, A., Binz, H. K., Forrer, P., Stumpp, M. T., Pliickthun, A., and Grutter, M. G. (2003). Designed to be stable Crystal structure of a consensus ankyrin repeat protein. Proc. Natl. Acad. Sci. 100, 1700-1705. 

Mosavi, L. K., Minor, D. L., Jr., and Peng, Z. Y. (2002). Consensus-derived structural determinants of the ankyrin repeat motif. Proc. Natl. Acad. Set. 99, 16029-16034. 

TRPA1 is the only member of the TRPA subbranch of the TRP gene family in mammals. This ion channel is characterized by a large number of ankyrin repeats ( 17) in its cytosolic N-terminus, a TRP channel membrane domain, and a short cytosolic C-terminal domain. The transcript of TRPA1 was initially identified in a cell line derived from a lung tumor (Jaquemar, Schenker et al. 1999). However, its functional role in these cells has not been studied further, and expression in lung tissue could not be confirmed. 

Code for a domain that interacts with the muscle ankyrin repeat proteins... 

Miller, M. K., Bang, M. L., and Witt, C. (2003). The muscle ankyrin repeat proteins CARP, ankrd2/Arpp and DARP as a family of titin filament based stress response molecules./ Mol. Biol. 333, 951-964. 

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