IPR042121
MutL, C-terminal domain, regulatory subdomain
InterPro entry
Short name | MutL_C_regsub |
Overlapping entries |
Description
The protein MutL is essential in mismatch repair as it coordinating multiple protein-protein interactions that signal strand removal upon mismatch recognition by MutS. MutL is composed of two structurally conserved domains connected by a variable flexible linker: an N-terminal ATPase domain and C-terminal dimerisation domain
[2]. The latter harbours the the endonuclease activity of the protein. Structural studies have shown that this C-terminal region is organized into a dimerization and a regulatory subdomain connected by a helical lever spanning the conserved endonuclease motif.
This superfamily represents the regulatory subdomain of the C-terminal domain of the MutL protein
[1].
References
1.Structure of the endonuclease domain of MutL: unlicensed to cut. Pillon MC, Lorenowicz JJ, Uckelmann M, Klocko AD, Mitchell RR, Chung YS, Modrich P, Walker GC, Simmons LA, Friedhoff P, Guarne A. Mol. Cell 39, 145-51, (2010). View articlePMID: 20603082
2.Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair. Guarne A, Ramon-Maiques S, Wolff EM, Ghirlando R, Hu X, Miller JH, Yang W. EMBO J. 23, 4134-45, (2004). View articlePMID: 15470502
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.30.1370.100