2a97
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(New page: 200px<br /> <applet load="2a97" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a97, resolution 1.80Å" /> '''Crystal structure o...)
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Revision as of 17:56, 29 October 2007
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Crystal structure of catalytic domain of Clostridium botulinum neurotoxin serotype F
Overview
The seven serologically distinct Clostridium botulinum neurotoxins (BoNTs, A-G) are zinc endopeptidases which block the neurotransmitter release by, cleaving one of the three proteins of the soluble, N-ethylmaleimide-sensitive-factor attachment protein receptor complex, (SNARE complex) essential for the fusion of vesicles containing, neurotransmitters with target membranes. These metallopeptidases exhibit, unique specificity for the substrates and peptide bonds they cleave., Development of countermeasures and therapeutics for BoNTs is a priority, because of their extreme toxicity and potential misuse as biowarfare, agents. Though they share sequence homology and structural similarity, the, structural information on each one of them is required to understand the, mechanism of action of all ... [(full description)]
About this Structure
2A97 is a [Single protein] structure of sequence from [Clostridium botulinum] with ZN and CD as [ligands]. Active as [[1]], with EC number [3.4.24.69]. Full crystallographic information is available from [OCA].
Reference
Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design., Agarwal R, Binz T, Swaminathan S, Biochemistry. 2005 Sep 6;44(35):11758-65. PMID:16128577
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