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The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.
Solbak, Sara M Reksten, Tove R Wray, Victor Bruns, Karsten Horvli, Ole Raae, Arnt J Henklein, Petra Henklein, Peter Röder, Rene Mitzner, David
Solbak, Sara M
Reksten, Tove R
Wray, Victor
Bruns, Karsten
Horvli, Ole
Raae, Arnt J
Henklein, Petra
Henklein, Peter
Röder, Rene
Mitzner, David
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Abstract
Cyclophilin A (CypA) represents a potential target for antiretroviral therapy since inhibition of CypA suppresses human immunodeficiency virus type 1 (HIV-1) replication, although the mechanism through which CypA modulates HIV-1 infectivity still remains unclear. The interaction of HIV-1 viral protein R (Vpr) with the human peptidyl prolyl isomerase CypA is known to occur in vitro and in vivo. However, the nature of the interaction of CypA with Pro-35 of N-terminal Vpr has remained undefined.
Citation
The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding. 2010, 10:31 BMC Struct. Biol.
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Journal
PubMed ID
PubMed Central ID
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Article
Language
en
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Series/Report no.
ISSN
1472-6807