Pyridine-based allosteric inhibitors selectively target HIV-1 integrase tetramers and exhibit enhanced antiviral activity against a dolutegravir resistant mutant virus indicating potential clinical benefits for combining these two classes of inhibitors.
A small molecule, cotransin, blocks transmembrane domains form integrating into cell membranes by allosterically ‘locking’ the lateral gate of the Sec61 translocation channel.
Identification of how bioactive lipids bind and inhibit glycine transporters has the potential to be exploited in the development of a new class of analgesics for chronic pain.
Interactions between viral RNA and the integrase enzyme are required for HIV-1 particles to become infectious, a process that can be disrupted through multiple mechanisms.
A transport mechanism is uncovered in the major drug-efflux system in E. coli involving two remote alternating-access conformational cycles, which could provide the basis for the development of allosteric inhibitors against multidrug resistance.