Purification and characterization of a protein with antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities from small brown-eyed cowpea seeds

2013 ◽  
Vol 60 (4) ◽  
pp. 393-398 ◽  
Author(s):  
Guo-Ting Tian ◽  
Meng Juan Zhu ◽  
Ying Ying Wu ◽  
Qin Liu ◽  
He Xiang Wang ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Purification And Characterization ◽  
Cowpea Seeds ◽  
Inhibitory Activities ◽  
Hiv 1

Purification and Characterization of HIV-1 Reverse Transcriptase Having a 1:1 Ratio of p66 and p51 Subunits

1994 ◽  
Vol 5 (6) ◽  
pp. 614-621 ◽  
Author(s):  
M. Stahlhut ◽  
Y. Li ◽  
J.H. Condra ◽  
J. Fu ◽  
L. Gotlib ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Purification And Characterization ◽  
Hiv 1

scholarly journals Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinantEscherichia coli

FEBS Letters ◽  
1990 ◽  
Vol 270 (1-2) ◽  
pp. 76-80 ◽  
Author(s):  
S.Patricia Becerra ◽  
G.Marius Clore ◽  
Angela M. Gronenborn ◽  
Anders R. Karlström ◽  
Stephen J. Stahl ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Rnase H ◽  
Purification And Characterization ◽  
Hiv 1

scholarly journals High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Betty Ha ◽  
Kevin P. Larsen ◽  
Jingji Zhang ◽  
Ziao Fu ◽  
Elizabeth Montabana ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Viral Entry ◽  
Reverse Transcription ◽  
Molecular Mechanisms ◽  
Dissociation Kinetics ◽  
Structural Mechanism ◽  
Medium Resolution ◽  
Kinetics Of ◽  
Hiv 1

AbstractReverse transcription of the HIV-1 viral RNA genome (vRNA) is an integral step in virus replication. Upon viral entry, HIV-1 reverse transcriptase (RT) initiates from a host tRNALys3 primer bound to the vRNA genome and is the target of key antivirals, such as non-nucleoside reverse transcriptase inhibitors (NNRTIs). Initiation proceeds slowly with discrete pausing events along the vRNA template. Despite prior medium-resolution structural characterization of reverse transcriptase initiation complexes (RTICs), higher-resolution structures of the RTIC are needed to understand the molecular mechanisms that underlie initiation. Here we report cryo-EM structures of the core RTIC, RTIC–nevirapine, and RTIC–efavirenz complexes at 2.8, 3.1, and 2.9 Å, respectively. In combination with biochemical studies, these data suggest a basis for rapid dissociation kinetics of RT from the vRNA–tRNALys3 initiation complex and reveal a specific structural mechanism of nucleic acid conformational stabilization during initiation. Finally, our results show that NNRTIs inhibit the RTIC and exacerbate discrete pausing during early reverse transcription.

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