2c0q
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(New page: 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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Revision as of 17:45, 29 October 2007
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NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN
Overview
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 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].
Reference
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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