phosphothreonine residue binding

Definition

Target type: molecularfunction

Binding to a phosphorylated threonine residue within a protein. [GOC:ai]

Phosphothreonine residue binding is a molecular function that involves the specific recognition and interaction of a protein or other molecule with a phosphorylated threonine residue. This type of binding plays a critical role in signal transduction pathways, protein-protein interactions, and the regulation of various cellular processes.

Phosphorylation of threonine residues is a reversible modification that can alter the conformation and activity of proteins. When a threonine residue is phosphorylated, it acquires a negative charge, which can create new binding sites for other molecules. These interactions can lead to changes in protein activity, localization, or stability.

Proteins that bind to phosphothreonine residues typically contain specific domains or motifs that recognize and interact with the phosphorylated threonine. These domains often include positively charged residues or hydrophobic pockets that can interact with the negatively charged phosphate group and the surrounding amino acids.

The binding of a protein to a phosphothreonine residue can have a variety of downstream effects. For example, it can:

* **Activate or inhibit the activity of the target protein**
* **Recruit other proteins to the complex**
* **Promote or prevent the degradation of the target protein**
* **Change the localization of the target protein**

In summary, phosphothreonine residue binding is a crucial molecular function that enables proteins to specifically interact with and regulate the activity of other molecules. This interaction plays a fundamental role in a wide range of cellular processes, from signal transduction to protein trafficking and gene expression.'
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Proteins (1)

Compounds (8)