Link: University of Iowa

How HIV-1 Tat hijacks pol II elongation

HIV-1, the causative agent for AIDS, makes use of host enzymes to accomplish steps in viral replication including the production of full length viral mRNA. In new work published in today’s issue of Nature, the laboratories of Tahir Tahirov (Nebraska Medical Center) and David Price have determined the crystal structure of HIV-1 Tat in complex with human P-TEFb. The structure reveals conformational changes that could not have been anticipated from structures of Tat or P-TEFb alone and suggests a potentially druggable surface for inhibition of viral replication. The work was performed by Nigar Babayeva and Tahirov in Nebraska and by Katayoun Varzavand, Jeffrey Cooper, Stanley Sedore and Price in the Department and has also been featured in Cell.

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