1eh8
BENZYLATED HUMAN O6-ALKYLGUANINE-DNA ALKYLTRANSFERASE
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OverviewOverview
Human O(6)-alkylguanine-DNA alkyltransferase (AGT), which directly, reverses endogenous alkylation at the O(6)-position of guanine, confers, resistance to alkylation chemotherapies and is therefore an active, anticancer drug target. Crystal structures of active human AGT and its, biologically and therapeutically relevant methylated and benzylated, product complexes reveal an unexpected zinc-stabilized helical bridge, joining a two-domain alpha/beta structure. An asparagine hinge couples the, active site motif to a helix-turn-helix (HTH) motif implicated in DNA, binding. The reactive cysteine environment, its position within a groove, adjacent to the alkyl-binding cavity and mutational analyses characterize, DNA-damage recognition and inhibitor specificity, support a, structure-based ... [(full description)]
About this StructureAbout this Structure
1EH8 is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Active as [[protein-cysteine_S-methyltransferase Methylated-DNA--[protein]-cysteine S-methyltransferase]], with EC number [2.1.1.63]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding., Daniels DS, Mol CD, Arvai AS, Kanugula S, Pegg AE, Tainer JA, EMBO J. 2000 Apr 3;19(7):1719-30. PMID:10747039 [[Category: Methylated-DNA--[protein]-cysteine S-methyltransferase]]
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