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Mismatch Repair System (MMR) corrects mutations arising from DNA replication that escape from DNA polymerase proofreading activity, and prevents recombination between partially homologue sequences (homeologue recombination) [1]. This system has been extensively characterized in E. coli where three main proteins, MutS-L-H, are responsible for lesion recognition and repair. MutS recognizes mispaired bases and recruits MutL, a matchmaker protein that coordinates the action of most of the proteins involved in repair [1]. This ternary complex (DNA-MutS-L) activates MutH endonuclease, which cleaves unmethylated GATC sites transiently generated during replication, allowing strand discrimination [2]. MutL homologues from several organisms that lack MutH, including eukaryotes and most bacteria, have been found to possess a latent endonuclease activity essential for DNA strand discrimination [3]. This activity is dependent on the integrity of a metal binding motif located within MutL C-terminal domain (CTD). This motif, and therefore endonuclease activity, is absent in E.Aflibercept (VEGF Trap) coli MutL [3,4,10].Vipivotide tetraxetan MutL belongs to the GHKL ATPase family, which includes gyrase GyrB, Hsp90, histidine kinases and MutL [11].PMID:36717102 All members of this family share a well conserved N-terminal domain (NTD) that contains an ATPase active site [12]. In MutL, this domain is connected by a linker to a non-conserved CTD dimerization domain [12]. Although this family lacks a conventional ATPase signature motif, it shares four conserved sequence motifs (I-IV), responsible for ATP binding [12]. ATP-binding induced conformational changes are involved in the signaling of these proteins physiological activity [11,13]. The crystal structure of LN40, the 40 kDa NTD from E. coli MutL (here on denominated EcNTD), as well as human and yeast NTD MutL homologues have been determined [124]. EcNTD is made up of two a/b hemi-domains, sub-domain I (res. 109) and subdomain II (res. 21031) [12]. Both sub-domains contain a portion of the ATP catalytic site, but this is mainly made up of the subdomain I. The first hemi-domain contains the four ATP binding motifs (I V) characteristic of the.
