Winifred W. Prosise

TL;DR: The scNS3-NS4A structure provides the first atomic view of polyprotein cis processing, and suggests autoinhibition and substrate-induced activation mechanisms for regulation of NS3 protease activity.

TL;DR: The structure of the human full-length IgG4 S228P anti-PD1 antibody pembrolizumab is reported, and this unusual Fc conformation suggests possible structural diversity between IgG subclasses and shows that use of isolated antibody fragments could mask potentially important interactions, owing to molecular flexibility.

TL;DR: Reconstructions of single-particle cryo-electron microscopy reconstructions of the insulin receptor ECD dimer with insulin suggest that recruitment of the α-CT helix upon binding of the first insulin changes the relative subdomain orientations and triggers downstream signal propagation.

TL;DR: A single‐chain recombinant form of the protease has been constructed in which NS4A residues 21‐32 were fused in frame to the amino terminus of the NS3 protease domain (residues 3ndash181) through a tetrapeptide linker.

TL;DR: The structures of both the native holo-HCV NS3/4A proteasedomain and the protease domain with a serine 139 to alanine (S139A) mutation were solved to high resolution and correlated with changes in the buried surface area upon binding the inhibitor to the active site.