scholarly journals Biochemical Characterization of Recombinant HIV-1 Reverse Transcriptase (rRT) as a Glycyrrhizin-Binding Protein and the CK-II-Mediated Stimulation of rRT Activity Potently Inhibited by Glycyrrhetinic Acid Derivative.

1998 ◽  
Vol 21 (12) ◽  
pp. 1282-1285 ◽  
Author(s):  
Shigeyoshi HARADA ◽  
Toshiro MAEKAWA ◽  
Eiji HANEDA ◽  
Yuko MORIKAWA ◽  
Nobuyuki NAGATA ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Acid Derivative ◽  
Biochemical Characterization ◽  
Binding Protein ◽  
Glycyrrhetinic Acid ◽  
Hiv 1 ◽  
Stimulation Of

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.

scholarly journals Biochemical Characterization of the TATA-binding Protein-Gal4 Activation Domain Complex

2000 ◽  
Vol 275 (41) ◽  
pp. 31914-31920 ◽  
Author(s):  
Yueqing Xie ◽  
Carilee Denison ◽  
Sang-Hwa Yang ◽  
David A. Fancy ◽  
Thomas Kodadek
Keyword(s):  
Biochemical Characterization ◽  
Binding Protein ◽  
Tata Binding Protein ◽  
Activation Domain ◽  
Gal4 Activation Domain

scholarly journals Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR

Science ◽  
1991 ◽  
Vol 251 (5001) ◽  
pp. 1597-1600 ◽  
Author(s):  
A Gatignol ◽  
A Buckler-White ◽  
B Berkhout ◽  
K. Jeang
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Tar Rna ◽  
Hiv 1
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