Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation

HIV-1 reverse transcriptase (RT), a critical enzyme of the HIV life cycle and an important drug target, undergoes complex and largely uncharacterized conformational rearrangements that underlie its asymmetric folding, dimerization and subunit-selective ribonuclease H domain (RH) proteolysis. In the...

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Autores principales: Zheng, Xunhai, Pedersen, Lars C., Gabel, Scott A., Mueller, Geoffrey A., Cuneo, Matthew J., DeRose, Eugene F., Krahn, Juno M., London, Robert E.
Formato: Artigo
Lenguaje:Inglês
Publicado: Oxford University Press 2014
Materias:
Structural Biology
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC4005681/
https://ncbi.nlm.nih.gov/pubmed/24574528
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gku143
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