1eh8: Difference between revisions
New page: left|200px<br /> <applet load="1eh8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eh8, resolution 2.50Å" /> '''BENZYLATED HUMAN O6... |
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==About this Structure== | ==About this Structure== | ||
1EH8 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EH8 OCA]]. | 1EH8 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Methylated-DNA--[protein]-cysteine_S-methyltransferase Methylated-DNA--[protein]-cysteine S-methyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EH8 OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10747039 10747039] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10747039 10747039] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Methylated-DNA--[protein]-cysteine S-methyltransferase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Daniels, D.S.]] | [[Category: Daniels, D.S.]] | ||
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[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:14:01 2007'' | ||
Revision as of 15:09, 30 October 2007
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BENZYLATED HUMAN O6-ALKYLGUANINE-DNA ALKYLTRANSFERASE
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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