The new compounds work by inhibiting the function of a viral enzyme, called reverse transcriptase, which is essential for HIV replication. The researchers report in the online journal eLife that high resolution images of viral crystal structures reveal the new inhibitors bind to both the “wild-type” and the mutant forms of the reverse transcriptase. Examinations of the structures and results from biochemical assays show that the new reverse transcriptase inhibitors, “were better able to adopt their shapes’’ to bind to mutant HIV reverse transcriptase than existing agents, said Yang Yang, a postdoctoral researcher in the laboratory of Yale professor and Nobel laureate Thomas A. Steitz and first author of the study. The work was done in collaboration with Professor Xinyong Liu’s group at Shandong University in China. The study was supported by the Howard Hughes Medical Institute and the National Institutes of Health. Reference: “Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-d]pyrimidine non-nucleoside inhibitors” by Yang Yang, Dongwei Kang, Laura A Nguyen, Zachary B Smithline, Christophe Pannecouque, Peng Zhan, Xinyong Liu and Thomas A Steitz, 25 July 2018, eLife.DOI: 10.7554/eLife.36340