TPR domain binding

Definition

Target type: molecularfunction

Binding to a tetratricopeptide repeat (TPR) domain of a protein, the consensus sequence of which is defined by a pattern of small and large hydrophobic amino acids and a structure composed of helices. [GOC:mah]

TPR domain binding is a molecular function characterized by the interaction between a protein containing a TPR (tetratricopeptide repeat) domain and another protein or molecule. TPR domains are highly conserved protein motifs consisting of 34 amino acid residues that fold into a helix-turn-helix structure. These repeats typically assemble into tandem arrays of two or more, forming elongated structures that serve as protein-protein interaction modules.

The TPR domain acts as a scaffold, providing a binding site for diverse target proteins. These targets can be involved in a wide range of cellular processes, including signal transduction, protein trafficking, and transcription regulation.

The binding of a target protein to the TPR domain can induce conformational changes in both proteins, leading to the activation or inactivation of downstream signaling pathways. This interaction is often highly specific, relying on a combination of surface residues and hydrophobic interactions to ensure the correct binding partner is selected.

The versatility of TPR domain binding makes it a crucial component of various cellular functions. The ability of TPR domains to bind to a diverse range of target proteins, including kinases, phosphatases, and transcription factors, allows for the modulation of various cellular processes.

Furthermore, TPR domains can be found in a variety of proteins, both in eukaryotes and prokaryotes, highlighting their evolutionary importance. The widespread presence of TPR domains across species suggests their fundamental role in maintaining cellular homeostasis and regulating key cellular processes.'
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Proteins (3)

Compounds (115)