The intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.

2.50
Hdl Handle:
http://hdl.handle.net/10033/124027
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
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.
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
Type:
Article
Language:
en
ISSN:
1472-6807
Appears in Collections:
Publications from RG Biophysical Analysis (BA)

Full metadata record

DC FieldValue Language
dc.contributor.authorSolbak, Sara Men
dc.contributor.authorReksten, Tove Ren
dc.contributor.authorWray, Victoren
dc.contributor.authorBruns, Karstenen
dc.contributor.authorHorvli, Oleen
dc.contributor.authorRaae, Arnt Jen
dc.contributor.authorHenklein, Petraen
dc.contributor.authorHenklein, Peteren
dc.contributor.authorRöder, Reneen
dc.contributor.authorMitzner, Daviden
dc.contributor.authorSchubert, Ulrichen
dc.contributor.authorFossen, Torgilsen
dc.date.accessioned2011-03-09T10:13:45Z-
dc.date.available2011-03-09T10:13:45Z-
dc.date.issued2010-
dc.identifier.citationThe intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding. 2010, 10:31 BMC Struct. Biol.en
dc.identifier.issn1472-6807-
dc.identifier.pmid20920334-
dc.identifier.doi10.1186/1472-6807-10-31-
dc.identifier.urihttp://hdl.handle.net/10033/124027-
dc.description.abstractCyclophilin 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.en
dc.language.isoenen
dc.subject.meshCyclophilin Aen
dc.subject.meshHumansen
dc.subject.meshKineticsen
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen
dc.subject.meshPeptidylprolyl Isomeraseen
dc.subject.meshProlineen
dc.subject.meshProtein Bindingen
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen
dc.subject.meshSurface Plasmon Resonanceen
dc.subject.meshVirus Replicationen
dc.subject.meshvpr Gene Products, Human Immunodeficiency Virusen
dc.titleThe intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.en
dc.typeArticleen
dc.contributor.departmentDepartment of Chemistry, University of Bergen, N-5007 Bergen, Norway.en
dc.identifier.journalBMC structural biologyen

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