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Many biological functions involve the formation of protein-protein complexes. Indeed, protein–protein interactions are considered to be the center of all functional living cells. Proteins can interact with each other by various structural, chemical and physical means. Some of these interactions can be highly specific, accompanied by high affinity, while some proteins are more flexible and bind diverse proteins as ligands. A common group of proteins that participate in protein-protein interactions and serve as multi-protein complex mediators are the tetra-trico-peptide repeat (TPR) proteins. TPR-containing proteins were found to be involved in many diverse processes in eukaryotic cells, including synaptic vesicle fusion (Young et al. 2003), peroxisomal targeting and import (Brocard et al. 2006; Fransen et al. 2008) and mitochondrial and chloroplast import (Baker et al. 2007; Mirus et al. 2009). In addition, TRPs are required for many bacterial pathways, such as outer membrane assembly (Gatsos et al. 2008), bio-mineralization of iron oxides in magnetotactic bacteria (Zeytuni et al. 2011) and pathogenesis ( Edqvist et al. 2006; Tiwari et al. 2009). In addition, mutations in TPR-containing proteins have been linked to a variety of human diseases, such as chronic granulomatous disease and Leber’s congenital amaurosis (D'Andrea & Regan 2003).

The TPR Motif as a Protein Interaction Module - A Discussion of Structure and Function