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20200415-drug-repurposing-reframe-covid19

April 15, 2020

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Members of the Law and Park labs during the recent International Symposium on Hepatitis C Virus, Flaviviruses and Related Viruses in Copenhagen. From left: Fang Chen, Yukiye Koide, Joseph Cruz, and Mansun Law.
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From left: K. Barry Sharpless, Ardem Patapoutian and Dr. Herbert Wertheim Credit: Scripps Research
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Ron Burkle Credit: Ron Burkle
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From left: Richard Ulevitch, professor emeritus at Scripps Research, and Rob Garbaccio, senior vice president at Merck. Credit: Scripps Research.
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A newly designed transmembrane peptide (blue) binds to the TLR4 (orange) transmembrane helix, blocking receptor dimerization and reducing LPS-driven NF-κB inflammatory signaling. Credit: Scripps Research
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Dissociation of the four-part TTR protein. The energy landscape shows stable states toward the bottom and unstable transition states toward the top. In the canonical pathway (red), the tetramer (T) dissociates via a native-like, compact transition state (‡1) into transient dimer intermediates (D) before full dissociation into monomers (M). In the newly discovered alternative pathway (blue), the tetramer dissociates through a more expanded transition state (‡2) directly into monomers. Credit: Jan-Hannes Schäfer, Scripps Research
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Scientists discover a new way that a disease-linked protein comes apart

Chemistry Integrative Structural & Computational Biology
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