Cargando…
Unfolding the HIV-1 reverse transcriptase RNase H domain – how to lose a molecular tug-of-war
Formation of the mature HIV-1 reverse transcriptase (RT) p66/p51 heterodimer requires subunit-specific processing of the p66/p66′ homodimer precursor. Since the ribonuclease H (RH) domain contains an occult cleavage site located near its center, cleavage must occur either prior to folding or subsequ...
Autores principales: | Zheng, Xunhai, Pedersen, Lars C., Gabel, Scott A., Mueller, Geoffrey A., DeRose, Eugene F., London, Robert E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4770237/ https://www.ncbi.nlm.nih.gov/pubmed/26773054 http://dx.doi.org/10.1093/nar/gkv1538 |
Ejemplares similares
-
Coordination between the polymerase and RNase H activity of HIV-1 reverse transcriptase
por: Figiel, Małgorzata, et al.
Publicado: (2017) -
Altered error specificity of RNase H-deficient HIV-1 reverse transcriptases during DNA-dependent DNA synthesis
por: Álvarez, Mar, et al.
Publicado: (2013) -
Transitions in DNA polymerase β μs-ms dynamics related to substrate binding and catalysis
por: DeRose, Eugene F, et al.
Publicado: (2018) -
Biochemical characterization of a multi-drug resistant HIV-1 subtype AG reverse transcriptase: antagonism of AZT discrimination and excision pathways and sensitivity to RNase H inhibitors
por: Schneider, Anna, et al.
Publicado: (2016) -
Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation
por: Zheng, Xunhai, et al.
Publicado: (2014)