On December 1, 1999, Barrett, Tracey E.; Scharer, Orlando D.; Savva, Renos; Brown, Tom; Jiricny, Josef; Verdine, Gregory L.; Pearl, Laurence H. published an article.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one The title of the article was Crystal structure of a thwarted mismatch glycosylase DNA repair complex. And the article contained the following:
The bacterial mismatch-specific uracil-DNA glycosylase (MUG) and eukaryotic thymine-DNA glycosylase (TDG) enzymes form a homologous family of DNA glycosylases that initiate base-excision repair of G:U/T mismatches. Despite low sequence homol., the MUG/TDG enzymes are structurally related to the uracil-DNA glycosylase enzymes, but have a very different mechanism for substrate recognition. We have now determined the crystal structure of the Escherichia coli MUG enzyme complexed with an oligonucleotide containing a non-hydrolysable deoxyuridine analog mismatched with guanine, providing the first structure of an intact substrate-nucleotide productively bound to a hydrolytic DNA glycosylase. The structure of this complex explains the preference for G:U over G:T mispairs, and reveals an essentially non-specific pyrimidine-binding pocket that allows MUG/TDG enzymes to excise the alkylated base, 3,N4-ethenocytosine. Together with structures for the free enzyme and for an abasic-DNA product complex, the MUG-substrate analog complex reveals the conformational changes accompanying the catalytic cycle of substrate binding, base excision and product release. The experimental process involved the reaction of Imidazo[1,2-c]pyrimidin-5(6H)-one(cas: 55662-66-3).Name: Imidazo[1,2-c]pyrimidin-5(6H)-one
The Article related to crystal structure uracil dna glycosylase complex, dna uracil glycosylase conformation repair mechanism, Enzymes: Structure-Conformation-Active Site and other aspects.Name: Imidazo[1,2-c]pyrimidin-5(6H)-one
Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem