Escherichia coli LysU is a potential surrogate for human lysyl tRNA synthetase in interactions with the C-terminal domain of HIV-1 capsid protein

2013 ◽  
Vol 11 (4) ◽  
pp. 612-620 ◽  
Author(s):  
Nonlawat Boonyalai ◽  
James R. Pullen ◽  
Mohd Firdaus Abdul Wahab ◽  
Michael Wright ◽  
Andrew D. Miller
Keyword(s):  
Escherichia Coli ◽  
Capsid Protein ◽  
Trna Synthetase ◽  
Terminal Domain ◽  
Hiv 1

scholarly journals Critical Role of Helix 4 of HIV-1 Capsid C-terminal Domain in Interactions with Human Lysyl-tRNA Synthetase

2007 ◽  
Vol 282 (44) ◽  
pp. 32274-32279 ◽  
Author(s):  
Brandie J. Kovaleski ◽  
Robert Kennedy ◽  
Ahmad Khorchid ◽  
Lawrence Kleiman ◽  
Hiroshi Matsuo ◽  
...  
Keyword(s):  
Critical Role ◽  
Trna Synthetase ◽  
Terminal Domain ◽  
Hiv 1

scholarly journals Production and purification of polymerization-competent HIV-1 capsid protein p24 (CA) in NiCo21(DE3) Escherichia coli

2013 ◽  
Vol 13 (1) ◽  
pp. 107 ◽  
Author(s):  
Sin Teow ◽  
Siti Mualif ◽  
Tasyriq Omar ◽  
Chew Wei ◽  
Narazah Yusoff ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Capsid Protein ◽  
Hiv 1

scholarly journals HIV-1 Virus Interactions With Host Proteins: Interaction of the N-terminal Domain of the HIV-1 Capsid Protein With Human Calmodulin

2019 ◽  
Vol 14 (5) ◽  
pp. 1934578X1984919
Author(s):  
Ywh-Min Tzou ◽  
Ronald Shin ◽  
N. Rama Krishna
Keyword(s):  
Capsid Protein ◽  
Host Factors ◽  
Host Proteins ◽  
Terminal Domain ◽  
Immunodeficiency Virus ◽  
Infected Cells ◽  
Virus Interactions ◽  
Precise Role ◽  
Hiv 1

The human immunodeficiency virus (HIV-1 virus) exploits several host factors for assembly, infection, and replication within the infected cells. In this work, we describe the evidence for an interaction of the N-terminal domain of the HIV-1 capsid protein with human calmodulin. The precise role of this interaction within the life cycle of the HIV-1 virus is yet to be defined. Potential roles for this interaction in the viral capsid uncoating are discussed.

scholarly journals A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein

Virology ◽  
2007 ◽  
Vol 359 (1) ◽  
pp. 105-115 ◽  
Author(s):  
Shixing Tang ◽  
Sherimay Ablan ◽  
Megan Dueck ◽  
Wilfredo Ayala-López ◽  
Brenda Soto ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Aromatic Residue ◽  
Terminal Domain ◽  
Hiv 1

scholarly journals 1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein

2009 ◽  
Vol 4 (1) ◽  
pp. 21-23 ◽  
Author(s):  
Jinwon Jung ◽  
In-Ja L. Byeon ◽  
Jinwoo Ahn ◽  
Jason Concel ◽  
Angela M. Gronenborn
Keyword(s):  
Capsid Protein ◽  
Terminal Domain ◽  
Hiv 1

Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein

FEBS Journal ◽  
2008 ◽  
Vol 275 (13) ◽  
pp. 3299-3311 ◽  
Author(s):  
Luis A. Alcaraz ◽  
Marta del Álamo ◽  
Mauricio G. Mateu ◽  
José L. Neira
Keyword(s):  
Capsid Protein ◽  
Terminal Domain ◽  
Structural Mobility ◽  
Hiv 1

The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor

2005 ◽  
Vol 12 (8) ◽  
pp. 678-682 ◽  
Author(s):  
François Ternois ◽  
Jana Sticht ◽  
Stéphane Duquerroy ◽  
Hans-Georg Kräusslich ◽  
Félix A Rey
Keyword(s):  
Capsid Protein ◽  
Protein C ◽  
Virus Assembly ◽  
Terminal Domain ◽  
Hiv 1
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