TTC1 Human

The TPR motif typically consists of a pair of antiparallel alpha helices. These helices fold together to produce a single, linear solenoid domain known as the TPR domain. The TPR motifs are usually found in tandem arrays of 3 to 16 motifs, which form scaffolds to mediate protein-protein interactions .

The TTC1 protein specifically binds to the Galpha subunit of G protein-coupled receptors to activate the Ras signaling pathway. This pathway is essential for various cellular processes, including cell growth, differentiation, and survival .

Proteins containing TPR motifs, such as TTC1, are involved in a wide range of biological processes. These include the regulation of the cell cycle, protein folding, and the assembly of protein complexes. For example, TPR-containing proteins are found in the anaphase-promoting complex (APC) subunits, NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, and mitochondrial import proteins .

Mutations or dysregulation of TPR-containing proteins, including TTC1, can lead to various diseases. For instance, TTC1 has been associated with Seckel Syndrome and Rumination Disorder . Understanding the structure and function of TTC1 and other TPR-containing proteins can provide insights into the mechanisms underlying these diseases and potentially lead to the development of targeted therapies.

Recombinant TTC1 protein is used in research to study its role in protein-protein interactions and signaling pathways. By expressing and purifying human recombinant TTC1, researchers can investigate its biochemical properties and interactions with other proteins. This research can contribute to a better understanding of cellular processes and the development of new therapeutic strategies.