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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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| Main Authors: | , , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Oxford University Press
2014
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| Assuntos: | |
| Acesso em linha: | 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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