| 53-BP1_Tudor | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 solution structure of the mouse 53bp1 fragment (residues 1463-1617) | |||||||||
| Identifiers | |||||||||
| Symbol | 53-BP1_Tudor | ||||||||
| Pfam | PF09038 | ||||||||
| Pfam clan | CL0049 | ||||||||
| InterPro | IPR015125 | ||||||||
| |||||||||
This domain consist of ten beta-strands and a carboxy-terminal alpha-helix. The amino-terminal five beta-strands and the C-terminal five beta-strands adopt folds that are identical to each other. The domain is essential for the recruitment of proteins to double stranded breaks in DNA, which is mediated by interaction with methylated Lys 79 of histone H3.[1]
References
edit- ^ Huyen Y, Zgheib O, Ditullio RA, Gorgoulis VG, Zacharatos P, Petty TJ, Sheston EA, Mellert HS, Stavridi ES, Halazonetis TD (November 2004). "Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks". Nature. 432 (7015): 406–411. doi:10.1038/nature03114. PMID 15525939.
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