2c0q

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Revision as of 20:45, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2c0q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c0q, resolution 2.50Å" /> '''NON-AGED FORM OF MO...)
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File:2c0q.gif


2c0q, resolution 2.50Å

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NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN

OverviewOverview

Organophosphorus compounds (OPs) interfere with the catalytic mechanism of, acetylcholinesterase (AChE) by rapidly phosphorylating the catalytic, serine residue. The inhibited enzyme can at least partly be reactivated, with nucleophilic reactivators such as oximes. The covalently attached OP, conjugate may undergo further intramolecular dealkylation or deamidation, reactions, a process termed "aging" that results in an enzyme considered, completely resistant to reactivation. Of particular interest is the, inhibition and aging reaction of the OP compound tabun since tabun, conjugates display an extraordinary resistance toward most reactivators of, today. To investigate the structural basis for this resistance, we, determined the crystal structures of Mus musculus AChE (mAChE) inhibited, by ... [(full description)]

About this StructureAbout this Structure

2C0Q is a [Single protein] structure of sequence from [Mus musculus] with NTJ and P6G as [ligands]. Active as [[1]], with EC number [3.1.1.7]. Full crystallographic information is available from [OCA].

ReferenceReference

Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase., Ekstrom F, Akfur C, Tunemalm AK, Lundberg S, Biochemistry. 2006 Jan 10;45(1):74-81. PMID:16388582

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