InterPro domain: IPR038487

The Mre11 complex is a multi-subunit nuclease that is composed of Mre11, Rad50 and Nbs1/Xrs2, and is involved in checkpoint signalling and DNA replication [ 1 ]. Mre11 has an intrinsic DNA-binding activity that is stimulated by Rad50 on its own or in combination with Nbs1 [ 2 ].

Mre11 dimerizes via phosphodiesterase domains flanked by a alpha/beta capping domain, process which creates a U-shaped particle with a broad DNA/Rad50 binding cleft [ 3 ]. This superfamily represents the Mre11 capping domain.

1. The Mre11 complex: at the crossroads of dna repair and checkpoint signalling. Nat. Rev. Mol. Cell Biol. 3, 317-27
2. A mechanistic basis for Mre11-directed DNA joining at microhomologies. Proc. Natl. Acad. Sci. U.S.A. 97, 6409-14
3. Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat. Struct. Mol. Biol. 19, 693-700