Tetra-trico-peptide repeat (TPR) domains are found in numerous proteins, where they serve as interaction modules and multiprotein complex mediators. TPRs can be found in all kingdoms of life and regulate diverse biological processes, such as organelle targeting and protein import, vesicle fusion, and biomineralization. This review considers the structural features of TPR domains that permit the great ligand-binding diversity of this motif, given that TPR-interacting partners display variations in both sequence and secondary structure. In addition, tools for predicting TPR-interacting partners are discussed, as are the abilities of TPR domains to serve as protein-protein interaction scaffolds in biotechnology and therapeutics
Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are st...
The tetratrico peptide repeat (TPR) is a 34 amino acid protein motif. Over 10000 TPRs have been ide...
A major goal in modern biophysics has been to thermodynamically characterize macromolecular systems ...
Tetra-trico-peptide repeat (TPR) domains are found in numerous proteins, where they serve as interac...
The tetratricopeptide repeat (TPR) motif is a protein-protein interaction module found in multiple ...
SummaryLinear repeat proteins often have high structural similarity and low (∼25%) pairwise sequence...
AbstractThe tetratricopeptide repeat (TPR) is a 34-amino acid α-helical motif that occurs in over 30...
The tetratricopeptide repeat (TPR) is a 34-aa alpha-helical motif that occurs in tandem arrays in a ...
Repeat proteins contain short, tandem array of simple structural motifs that stack together to form ...
The tetratricopeptide repeat (TPR) motif is a protein-protein interaction module that acts as an org...
Tetratricopeptide (TPR) repeats are a 34-residue helix-turn-helix motif that when repeated pack into...
Tetratricopeptide repeat (TPR) is a solenoid repeat protein facilitating various protein interaction...
The tetratricopeptide repeat (TPR) is a 34-amino acid alpha-helical motif that occurs in over 300 di...
International audienceThe tetratricopeptide motif repeat (TPR) is an α-helix-turn-α-helix motif that...
Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are st...
Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are st...
The tetratrico peptide repeat (TPR) is a 34 amino acid protein motif. Over 10000 TPRs have been ide...
A major goal in modern biophysics has been to thermodynamically characterize macromolecular systems ...
Tetra-trico-peptide repeat (TPR) domains are found in numerous proteins, where they serve as interac...
The tetratricopeptide repeat (TPR) motif is a protein-protein interaction module found in multiple ...
SummaryLinear repeat proteins often have high structural similarity and low (∼25%) pairwise sequence...
AbstractThe tetratricopeptide repeat (TPR) is a 34-amino acid α-helical motif that occurs in over 30...
The tetratricopeptide repeat (TPR) is a 34-aa alpha-helical motif that occurs in tandem arrays in a ...
Repeat proteins contain short, tandem array of simple structural motifs that stack together to form ...
The tetratricopeptide repeat (TPR) motif is a protein-protein interaction module that acts as an org...
Tetratricopeptide (TPR) repeats are a 34-residue helix-turn-helix motif that when repeated pack into...
Tetratricopeptide repeat (TPR) is a solenoid repeat protein facilitating various protein interaction...
The tetratricopeptide repeat (TPR) is a 34-amino acid alpha-helical motif that occurs in over 300 di...
International audienceThe tetratricopeptide motif repeat (TPR) is an α-helix-turn-α-helix motif that...
Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are st...
Consensus-designed tetratricopeptide repeat proteins are highly stable, modular proteins that are st...
The tetratrico peptide repeat (TPR) is a 34 amino acid protein motif. Over 10000 TPRs have been ide...
A major goal in modern biophysics has been to thermodynamically characterize macromolecular systems ...