A diverse view of protein dynamics from NMR studies of HIV-1 protease flaps

2007 ◽  
Vol 70 (4) ◽  
pp. 1408-1415 ◽  
Author(s):  
Rieko Ishima ◽  
John M. Louis
Keyword(s):  
Protein Dynamics ◽  
Nmr Studies ◽  
Hiv 1

scholarly journals Solid-State NMR Studies of HIV-1 Capsid Protein Assemblies

2010 ◽  
Vol 132 (6) ◽  
pp. 1976-1987 ◽  
Author(s):  
Yun Han ◽  
Jinwoo Ahn ◽  
Jason Concel ◽  
In-Ja L. Byeon ◽  
Angela M. Gronenborn ◽  
...  
Keyword(s):  
Solid State ◽  
Capsid Protein ◽  
Solid State Nmr ◽  
Protein Assemblies ◽  
Nmr Studies ◽  
Hiv 1

NMR Studies of the Phosphorylation Motif of the HIV-1 Protein Vpu Bound to the F-Box Protein β-TrCP†

Biochemistry ◽  
2003 ◽  
Vol 42 (50) ◽  
pp. 14741-14751 ◽  
Author(s):  
Gaël Coadou ◽  
Josyane Gharbi-Benarous ◽  
Simon Megy ◽  
Gildas Bertho ◽  
Nathalie Evrard-Todeschi ◽  
...  
Keyword(s):  
Nmr Studies ◽  
Phosphorylation Motif ◽  
F Box Protein ◽  
Hiv 1

scholarly journals 19F NMR Studies of Cyclophilin a and its Interaction with HIV-1 Capsid

2020 ◽  
Vol 118 (3) ◽  
pp. 503a
Author(s):  
Manman Lu ◽  
Tatyana E. Polenova ◽  
Angela M. Gronenborn
Keyword(s):  
Cyclophilin A ◽  
19F Nmr ◽  
Nmr Studies ◽  
Hiv 1

scholarly journals Identification of the initial nucleocapsid recognition element in the HIV-1 RNA packaging signal

2020 ◽  
Vol 117 (30) ◽  
pp. 17737-17746 ◽  
Author(s):  
Pengfei Ding ◽  
Siarhei Kharytonchyk ◽  
Alexis Waller ◽  
Ugonna Mbaekwe ◽  
Sapna Basappa ◽  
...  
Keyword(s):  
Binding Sites ◽  
Virus Assembly ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Nmr Studies ◽  
Recognition Element ◽  
High Affinity ◽  
Molecule Inhibitor ◽  
Encapsidation Signal ◽  
Hiv 1

Selective packaging of the HIV-1 genome during virus assembly is mediated by interactions between the dimeric 5ʹ-leader of the unspliced viral RNA and the nucleocapsid (NC) domains of a small number of assembling viral Gag polyproteins. Here, we show that the dimeric 5′-leader contains more than two dozen NC binding sites with affinities ranging from 40 nM to 1.4 μM, and that all high-affinity sites (Kd≲ 400 nM) reside within a ∼150-nt region of the leader sufficient to promote RNA packaging (core encapsidation signal, ΨCES). The four initial binding sites with highest affinity reside near two symmetrically equivalent three-way junction structures. Unlike the other high-affinity sites, which bind NC with exothermic energetics, binding to these sites occurs endothermically due to concomitant unwinding of a weakly base-paired [UUUU]:[GGAG] helical element. Mutations that stabilize base pairing within this element eliminate NC binding to this site and severely impair RNA packaging into virus-like particles. NMR studies reveal that a recently discovered small-molecule inhibitor of HIV-1 RNA packaging that appears to function by stabilizing the structure of the leader binds directly to the [UUUU]:[GGAG] helix. Our findings suggest a sequential NC binding mechanism for Gag-genome assembly and identify a potential RNA Achilles’ heel to which HIV therapeutics may be targeted.

NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein β-TrCP

Peptides ◽  
2006 ◽  
Vol 27 (1) ◽  
pp. 194-210 ◽  
Author(s):  
Nathalie Evrard-Todeschi ◽  
Josyane Gharbi-Benarous ◽  
Gildas Bertho ◽  
Gaël Coadou ◽  
Simon Megy ◽  
...  
Keyword(s):  
Nmr Studies ◽  
F Box Protein ◽  
Hiv 1
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