The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.
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Authors
Solbak, Sara MReksten, Tove R
Wray, Victor
Bruns, Karsten
Horvli, Ole
Raae, Arnt J
Henklein, Petra
Henklein, Peter
Röder, Rene
Mitzner, David
Schubert, Ulrich
Fossen, Torgils
Issue Date
2010
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Show full item recordAbstract
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.Affiliation
Department of Chemistry, University of Bergen, N-5007 Bergen, Norway.Journal
BMC structural biologyPubMed ID
20920334Type
ArticleLanguage
enISSN
1472-6807ae974a485f413a2113503eed53cd6c53
10.1186/1472-6807-10-31
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