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TUDOR Domain
Structure:

No ImageThe three-dimensional structure of the Tudor domain of human SMN forms a strongly bent anti-parallel beta-sheet consisting five beta-strands that form a barrel-like fold. Several amino acids residues stabilize the SMN Tudor domain structure through formation of a hydrophobic core and are conserved among other Tudor domain sequences suggesting that other Tudor domains possess a similar three-dimensional fold. Interestingly, the structure of the SMN Tudor domain resembles the fold of the Sm core proteins despite an absence of any amino acid sequence similarity.
Structure Reference:
Huang, Y. et al. (2006) Science. 312(5774): 748-51. PDB: 2GFA.

 


Domain binding and function:
The Tudor domain was originally identified as a region of 50 amino acids found in the Tudor protein (a posterior group gene) encoded in Drosophila. The three-dimensional structure of the Tudor domain of human SMN forms a strongly bent anti-parallel β-sheet consisting of five β-strands with a barrel-like fold.  It was subsequently found among other proteins to be involved in binding RNA.  Two additional Tudor domain containing proteins, 53BP1 and JMJD2A contain either tandem or double Tudor domains with distinct folds despite sequence similarity.  The unusual folds of these proteins are required for its ability to recognize methylated histones. 
Examples of Proteins: 
TUDOR domain proteins        Binding Partner
SMN     methylated RG repeats of Sm proteins
53BP1     methylated H4-K20
JMJD2A
     methylated H3-K4, H4-K20


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