1m3q
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(New page: 200px<br /> <applet load="1m3q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3q, resolution 1.90Å" /> '''Crystal Structure o...)
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Revision as of 16:00, 12 November 2007
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Crystal Structure of hogg1 D268E Mutant with Base-Excised DNA and 8-aminoguanine
Contents |
Overview
DNA glycosylase/lyases initiate the repair of damaged nucleobases in the, genome by catalyzing excision of aberrant nucleobases and nicking of the, lesion-containing DNA strand. Nearly all of these proteins have the, unusual property of remaining tightly bound in vitro to the end products, of the reaction cascade. We have taken advantage of this property to, crystallize and structurally characterize the end product resulting from, complete DNA processing by a catalytically active mutant form of human, 8-oxoguanine DNA glycosylase (D268E hOgg1). The resulting structure is, consistent with the currently accepted catalytic mechanism for the, protein. Unexpectedly, however, soaking of a nucleobase analog into the, crystals results in religation of the DNA backbone in situ.
Disease
Known disease associated with this structure: Renal cell carcinoma, clear cell, somatic OMIM:[601982]
About this Structure
1M3Q is a Single protein structure of sequence from Homo sapiens with CA and ANG as ligands. Full crystallographic information is available from OCA.
Reference
Structures of end products resulting from lesion processing by a DNA glycosylase/lyase., Chung SJ, Verdine GL, Chem Biol. 2004 Dec;11(12):1643-9. PMID:15610848
Page seeded by OCA on Mon Nov 12 18:06:49 2007
Categories: Homo sapiens | Single protein | Chung, S.J. | Verdine, G.L. | ANG | CA | 8-aminoguanine | 8-oxoguanine | Dna glycosylase | Dna repair | End product | Hogg | Re-ligation