Tetratricopeptide repeats

Ma, Q. and Whitlock, J. P., A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to... 

Das, a. K., P. W. Cohen, and D. Bareord, The structure of the tetratricopeptide repeats of protein phosphatase 5 implications for TPR-mediated protein-protein interactions. EmboJ, 1998, 17(5), 1192-9. 

Ballinger, C. A., P. Connell, Y. Wu, Z. Hu, L. J. Thompson, L. Y. Yin, and C. Patterson. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol. 19 4535-45.1999. 

Silverstein, A. M., N. Grammatikakis, B. H. Cochran, M. Chinkers, and W. B. Pratt. p50(cdc37) binds directly to the catalytic domain ofRafas well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site. J Biol Chem. 273 20090-5.1998. 

Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ. 2004. Human Sgtl binds HSP90 through the CHORD-Sgtl domain and not the tetratricopeptide repeat domain. J Biol Chem 279(16) 16511-16517. 

Kreppel LK, Hart GW. Regulation of a cytosolic and nuclear O-GIcNAc transferase. Role of the tetratricopeptide repeats. J. Biol. Chem. 1999 274 32015-32022. 

Kobayashi, K., Sueyoshi, T., Inoue, K., Moore, R. and Negishi, M. (2003) Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells. Molecular Pharmacology, 64, 1069-1075. 

Fig. 5. Domain structure of Hsp70 co-chaperones. Individual domains/modules are represented by differendy shaded boxes. The known structural features and functions of domains are indicated. The following abbreviations for the different domains were used NLS, nuclear localization sequence TRSEEX, Thr-Arg-Ser-Glu-Glu-Xaa repeat motif Ub, ubiquitin-like domain Bag, Bag homology region WW, Trp-Trp domain TPR, tetratricopeptide repeat GGMP, Gly-Gly-Met-Pro repeat motif +/—, charged region U box, U box motif of E4 ubiquitin ligases DnaK, interaction site for DnaK 70, interaction site for Hsp70 90, interaction site for Hsp90.

TETRATRICOPEPTIDE REPEATS OF TFC4 AND A LIMITING STEP IN THE ASSEMBLY OF THE INITIATION FACTOR TFIIIB... 

The most prominent structural feature of Tfc4 is its 11 tetratricopeptide repeats (Marek et al., 1993 Rameau et al., 1994). TPRs are ubiquitous elements of protein structure that function as sites of protein-protein interaction (Lamb et al., 1995). The motif is defined by a degenerate sequence, usually 34 amino acids in length, that is most often found in tandem arrays (Lamb et al., 1995). Individual TPRs fold into two antiparallel a-helices, designated A and B, which are separated by a short turn. The helices within each repeat stack together with helices in adjacent... 

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