1eh6
From Proteopedia
(New page: 200px<br /> <applet load="1eh6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eh6, resolution 2.00Å" /> '''HUMAN O6-ALKYLGUANI...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1EH6 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=1EH6 OCA]]. | + | 1EH6 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=1EH6 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 14:14:04 2007'' |
Revision as of 12:09, 30 October 2007
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HUMAN O6-ALKYLGUANINE-DNA ALKYLTRANSFERASE
Overview
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 Structure
1EH6 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].
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:10747039[[Category: Methylated-DNA--[protein]-cysteine S-methyltransferase]]
Page seeded by OCA on Tue Oct 30 14:14:04 2007
