Volume 27 Issue 7, July 2020

Insights from structural biology lead to the development of mini-Ins—a human des-octapeptide insulin analog that is monomeric and has receptor binding affinity and in vitro and in vivo activities comparable to those of human insulin.

Cryo-EM structures of a C. elegans cGMP-activated channel TAX-4 in lipid nanodiscs reveal a hydrophobic gate in the central cavity and, together with electrophysiology, provide mechanistic insights into the gating and regulation of CNG channels.

Cryo-EM structures of TRPV3 in nanodiscs reveal lipids bound to the channel and unprecedented conformations of the selectivity filter and of the pore-lining helix S6, underscoring the importance of lipids for the channel structure.

A cryo-EM structure of mouse TRPV3 in nanodiscs reveal lipids bound to the pore domain, stabilizing the selectivity filter in the narrow state and the S6 in a π-helical conformation.

A cryo-EM structure of in vitro−formed fibrils of the human islet amyloid polypeptide (hIAPP) suggests both why the mutation S20G promotes aggregation and a potential basis for cross-seeding with β-amyloid, and leads to the design of peptide inhibitors.

Cryo-EM analyses of amyloid fibrils formed by synthetic human IAPP show an S-fold for the main polymorph, with the backbone superimposable with those of amyloid-β fibrils in antiparallel arrangement.

Cryo-EM elucidation of a fully reconstituted Pol II–DSF–PAF1–SPT6 elongation complex defines the position of PAF1 subunit RTF1 and reveals contacts with the Pol II bridge helix that may allosterically stimulate transcription elongation.

RBS-ID, a method to identify RNA–protein interactions by crosslinking, uses hydrofluoride to cleave RNA to simple mono-nucleoside adducts, which improves coverage and resolution of RNA binding site identification.