H
IPR042121

MutL, C-terminal domain, regulatory subdomain

InterPro entry
Short nameMutL_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

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