Journal:JBSD:28
From Proteopedia
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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 binding site of Sirt1 refers to a series of residues (colored in green) and key active residue (colored in magenta) in the catalytic domain indicated by Federico’s et al study. | 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 binding site of Sirt1 refers to a series of residues (colored in green) and key active residue (colored in magenta) in the catalytic domain indicated by Federico’s et al study. | ||
| - | In silico results indicate that traditional Chinese medicine compounds <scene name='Journal:JBSD:28/Cv/4'>(S)-tryptophan-betaxanthin</scene> (colored in purple), 5-O-feruloylquinic acid (colored in orange), and RosA (colored in yellow) 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> (colored in purple), <scene name='Journal:JBSD:28/Cv/5'>5-O-feruloylquinic acid</scene> (colored in orange), and RosA (colored in yellow) 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. |
</StructureSection> | </StructureSection> | ||
Revision as of 14:08, 24 October 2012
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
