Tudor domain

A Tudor domain is a conserved protein domain that was originally identified as a 50 amino acid region in the Tudor protein of Drosophila. The corresponding, structurally characterized Tudor domain in the human SMN protein (SMN = survival of motor neuron ) consists of five antiparallel β -sheets with a barrel-like ( "barrel -like" ) folding. This domain recognizes symmetrically methylated arginine.

The proteins TP53BP1 (Tumor suppressor p53 -binding protein 1 ) and its homologue in the fission yeast CRB2 and JMJD2A ( Jumonji domain containing 2A) containing either tandem or double Tudor domains and recognize methylated histones.

It was also found that Tudor domain play a role in RNA binding. The structural basis of ligand binding is not yet understood. More Tudor domain proteins are AKAP1 (A- kinase anchor protein 1) and ARID4A (AT rich interactive domain 4A), and others.