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• W3215638063 abstract "Tuberculosis drug resistance continues to threaten global health but the underline molecular mechanisms are not clear. Ethambutol (EMB), one of the well-known first - line drugs in tuberculosis treatment is, unfortunately, not free from drug resistance problems. Genomic studies have shown that some genetic mutations in Mycobacterium tuberculosis (Mtb) EmbR, and EmbC/A/B genes cause EMB resistance. EmbR-PknH pair controls embC/A/B operon, which encodes EmbC/A/B genes, and EMB interacts with EmbA/B proteins. However, the EmbR binding site on PknH was unknown. We conducted molecular simulation on the EmbR- peptides binding structures and discovered phosphorylated PknH 273-280 (N'-HEALSPDPD-C') makes β strand with the EmbR FHA domain, as β-MoRF (MoRF; molecular recognition feature) does at its binding site. Hydrogen bond number analysis also supported the peptides' β-MoRF forming activity at the EmbR FHA domain. Also, we discovered that previously known phosphorylation residues might have their chronological order according to the phosphorylation status. The discovery validated that Mtb PknH 273-280 (N'-HEALSDPD-C') has reliable EmbR binding affinity. This approach is revolutionary in the computer-aided drug discovery field, because it is the first trial to discover the protein-protein interaction site, and find binding partner in nature from this site." @default.
• W3215638063 created "2021-12-06" @default.
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• W3215638063 date "2021-12-01" @default.
• W3215638063 modified "2023-10-18" @default.
• W3215638063 title "Computational prediction and validation of specific EmbR binding site on PknH" @default.
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• W3215638063 doi "https://doi.org/10.1016/j.synbio.2021.11.006" @default.
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