Journal:JBSD:28
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<scene name='Journal:JBSD:28/Cv/2'>Silent information regulator 1 (Sirt1)</scene> is classified as nicotinamide adenine dinucleotide (NAD)-dependent histone deacetylase. It catalyzes the deacetylation reaction of proteins and cleavage of NAD into nicotinamide and 1-O-acetyl-ADP ribose, which plays an important role in regulating metabolic signaling pathways in various organisms. Sirt1 is a potential target protein for diseases associated with aging. | <scene name='Journal:JBSD:28/Cv/2'>Silent information regulator 1 (Sirt1)</scene> is classified as nicotinamide adenine dinucleotide (NAD)-dependent histone deacetylase. It catalyzes the deacetylation reaction of proteins and cleavage of NAD into nicotinamide and 1-O-acetyl-ADP ribose, which plays an important role in regulating metabolic signaling pathways in various organisms. Sirt1 is a potential target protein for diseases associated with aging. | ||
| - | The structure of Sirt1 protein for virtual screening is generated using Homology Modeling with the sequence of Human Sirt1 (UniProtKB: Q96EB6) and the template proteins of Human SirT2 (PDB: [[1j8f]]), Human SirT5 (PDB: [[2nyr]]), ''Archaeoglobus fulgidus'' Sir2 (PDB: [[1ici]]), Yeast Sir2 (PDB: [[1q17]]), and the protein produced by I-TASSER. The definition of <scene name='Journal:JBSD:28/Cv/7'>binding site of Sirt1 refers to a series of residues</scene> (<span style="color:lime;background-color:black;font-weight:bold;">colored in green</span>) and key active residue (<font color='magenta'><b>colored in magenta</b></font>) in the catalytic domain indicated by Federico’s et al study <ref name="Medda">PMID: 19419202</ref>. | + | The structure of Sirt1 protein for virtual screening is generated using Homology Modeling with the sequence of Human Sirt1 (UniProtKB: Q96EB6) and the template proteins of Human SirT2 (PDB: [[1j8f]]), Human SirT5 (PDB: [[2nyr]]), ''Archaeoglobus fulgidus'' Sir2 (PDB: [[1ici]]), Yeast Sir2 (PDB: [[1q17]]), and the protein produced by I-TASSER. The definition of <scene name='Journal:JBSD:28/Cv/7'>binding site of Sirt1 refers to a series of residues</scene> (<span style="color:lime;background-color:black;font-weight:bold;">colored in green</span>) and key active residue (<font color='magenta'><b>colored in magenta</b></font>) in the catalytic domain indicated by Federico’s ''et al'' study <ref name="Medda">PMID: 19419202</ref>. |
In silico results indicate that traditional Chinese medicine compounds <scene name='Journal:JBSD:28/Cv/4'>(S)-tryptophan-betaxanthin</scene> (<font color='purple'><b>colored in purple</b></font>), <scene name='Journal:JBSD:28/Cv/6'>5-O-feruloylquinic acid</scene> (<span style="color:orange;background-color:black;font-weight:bold;">colored in orange</span>), and <scene name='Journal:JBSD:28/Cv/10'>RosA</scene> (<span style="color:yellow;background-color:black;font-weight:bold;">colored in yellow</span>) had high binding affinity with Sirt1 protein and formed hydrogen bonds with residue Ser442 and other residues in the Sirt1 binding site (colored in cyan). The top TCM candidates, (S)-tryptophan-betaxanthin, 5-O-feruloylquinic acid, and RosA, may have potential to be lead compounds for diseases associated with aging. | In silico results indicate that traditional Chinese medicine compounds <scene name='Journal:JBSD:28/Cv/4'>(S)-tryptophan-betaxanthin</scene> (<font color='purple'><b>colored in purple</b></font>), <scene name='Journal:JBSD:28/Cv/6'>5-O-feruloylquinic acid</scene> (<span style="color:orange;background-color:black;font-weight:bold;">colored in orange</span>), and <scene name='Journal:JBSD:28/Cv/10'>RosA</scene> (<span style="color:yellow;background-color:black;font-weight:bold;">colored in yellow</span>) had high binding affinity with Sirt1 protein and formed hydrogen bonds with residue Ser442 and other residues in the Sirt1 binding site (colored in cyan). The top TCM candidates, (S)-tryptophan-betaxanthin, 5-O-feruloylquinic acid, and RosA, may have potential to be lead compounds for diseases associated with aging. | ||
Revision as of 10:23, 25 October 2012
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- ↑ REF
- ↑ Medda F, Russell RJ, Higgins M, McCarthy AR, Campbell J, Slawin AM, Lane DP, Lain S, Westwood NJ. Novel cambinol analogs as sirtuin inhibitors: synthesis, biological evaluation, and rationalization of activity. J Med Chem. 2009 May 14;52(9):2673-82. PMID:19419202 doi:10.1021/jm8014298
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