title: Mismatch repair: the praying hands of fidelity.
abstract: High-resolution crystal structures have recently been solved for the mismatch binding protein MutS of Escherichia coli and its Thermus aquaticus homologue; they show how these factors recognise such structurally diverse substrates as base-base mismatches and insertion/deletion loops.
authors.affiliation: Institute of Medical Radiobiology of the University of Zürich and the Paul Scherrer Institute, August Forel-Strasse 7, CH-8008, Zürich, Switzerland. jiricny@imr.unizh.ch
authors.forename: J
authors.initials: J
authors.lastname: Jiricny
mesh_terms: D000251:Adenosine Triphosphatases; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D020137:Base Pair Mismatch; D004260:DNA Repair; D004268:DNA-Binding Proteins; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; D008958:Models, Molecular; D051719:MutS DNA Mismatch-Binding Protein; D020836:Protein Structure, Quaternary; D013824:Thermus / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D046911:Macromolecular Substances; D000251:Adenosine Triphosphatases; D051719:MutS DNA Mismatch-Binding Protein; C497175:MutS protein, E coli