Team:Goettingen/Team/DAC
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<p>Another approach of our project is the determination of the 3D structure of diadenylate cyclase (DAC) from the human pathogen <i>Listeria moncytogenes</i> by crystallography.</p> | <p>Another approach of our project is the determination of the 3D structure of diadenylate cyclase (DAC) from the human pathogen <i>Listeria moncytogenes</i> by crystallography.</p> | ||
- | <p> | + | <p>Once having a 3D structure of a protein in hand potential inhibitor binding sites can be identified by computational modeling. These chemical compounds may interfere with the activity of the cyclase and could therefore be used as a potential starting point for further drug development.</p> |
- | <p>Due to the fact that the diadenylate cyclase from Bacillus subtilis is difficult to crystallize, the full length protein from <i>Listeria</i> is going to be isolated and crystallized. Furthermore, <i>Streptococcus</i> and <i>Staphylococcus</i> will be used to obtain only the DAC domain of the protein for our analysis.</p> | + | <p>Due to the fact that the diadenylate cyclase from <i>Bacillus subtilis</i> is difficult to crystallize, the full length protein from <i>Listeria</i> is going to be isolated and crystallized. Furthermore, <i>Streptococcus</i> and <i>Staphylococcus</i> will be used to obtain only the DAC domain of the protein for our analysis.</p> |
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Revision as of 08:39, 27 September 2013