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Helmholtz Zentrum für Infektionsforschung Repository > Division of Molekulare Strukurbiologie (MOSB) > RG Biophysical Analysis (BA) > Publications from RG Biophysical Analysis (BA) > The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.


Please use this identifier to cite or link to this item: http://hdl.handle.net/10033/124027
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Title: The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.
Authors: Solbak, Sara M
Reksten, Tove R
Wray, Victor
Bruns, Karsten
Horvli, Ole
Raae, Arnt J
Henklein, Petra
Henklein, Peter
Röder, Rene
Mitzner, David
Schubert, Ulrich
Fossen, Torgils
Affiliation: Department of Chemistry, University of Bergen, N-5007 Bergen, Norway.
Citation: The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding. 2010, 10:31 BMC Struct. Biol.
Journal: BMC structural biology
Issue Date: 2010
URI: http://hdl.handle.net/10033/124027
DOI: 10.1186/1472-6807-10-31
PubMed ID: 20920334
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.
Type: Article
Language: en
MeSH: Cyclophilin A
Humans
Kinetics
Nuclear Magnetic Resonance, Biomolecular
Peptidylprolyl Isomerase
Proline
Protein Binding
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Surface Plasmon Resonance
Virus Replication
vpr Gene Products, Human Immunodeficiency Virus
ISSN: 1472-6807
Appears in Collections: Publications from RG Biophysical Analysis (BA)

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