fletcherlab.bsky.social
We investigate interesting E3 mechanisms at the frontline between virus and cell, with some virology thrown in for good measure. Ub-er fun! At the MRC-University of Glasgow Centre for Virus Research. https://thefletcherlab.co.uk
👤 Joined on 12 November 2024
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@e3ligase.bsky.social@e3ligase.bsky.social → @fletcherlab.bsky.socialA huge thank you to @clausenlab.bsky.social and the whole Clausen lab, as well as our great collaborators @fletcherlab.bsky.social and Elisabeth Tournier-Lasserve and team who made this work possible, and to everyone that made my PhD such a great time! doi.org/10.64898/202...
Show PostUsing cryo-EM, we showed that RNF213 forms a zinc-dependent 1.2 MDa dimer, occluding the E2 binding site and catalytic RZ domain to keep the E3 ligase inactive.
Show PostHappy to share my PhD work on the regulatory mechanism of E3 ligase RNF213! RNF213 is not a monomer, but a dimer that switches between inhibited and activated states in an ATP-dependent manner. We tracked the activation mechanism and showed how disease mutations can destabilize the inhibited state.
Show PostThank you @fletcherlab.bsky.social! And it was so wonderful to meet you this week!
Show PostHow do human cells defend against viruses? @sgfern.bsky.social discovers that human immune proteins named ISGs target ancient features of replication shared between animal and bacterial viruses – opening analysis of human immunity to the power of bacterial genetics www.biorxiv.org/content/10.6...
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