000062891 001__ 62891
000062891 005__ 20200402210514.0
000062891 0247_ $$2pmid$$apmid:18186541
000062891 0247_ $$2DOI$$a10.1002/psc.1004
000062891 0247_ $$2WOS$$aWOS:000257725000004
000062891 037__ $$aPreJuSER-62891
000062891 041__ $$aeng
000062891 082__ $$a570
000062891 084__ $$2WoS$$aBiochemistry & Molecular Biology
000062891 084__ $$2WoS$$aChemistry, Analytical
000062891 1001_ $$0P:(DE-Juel1)VDB28257$$aWittlich, M.$$b0$$uFZJ
000062891 245__ $$aStructural Consequences of Phosphorylations of two Serine Residues in the Cytoplasmic Domain of HIV-1 VpU
000062891 260__ $$aNew York, NY [u.a.]$$bWiley$$c2008
000062891 300__ $$a804 - 810
000062891 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000062891 3367_ $$2DataCite$$aOutput Types/Journal article
000062891 3367_ $$00$$2EndNote$$aJournal Article
000062891 3367_ $$2BibTeX$$aARTICLE
000062891 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000062891 3367_ $$2DRIVER$$aarticle
000062891 440_0 $$018981$$aJournal of Peptide Science$$v14$$x1075-2617
000062891 500__ $$aRecord converted from VDB: 12.11.2012
000062891 520__ $$aThe human immunodeficiency virus type 1 (HIV-1) protein U (VpU) is an accessory protein responsible for enhancement of viral particle release and down regulation of the T-lymphocyte coreceptor CD4. Direct binding between the cytoplasmic domains of CD4 and VpU as well as phosphorylation of serines 53 and 57 in the cytoplasmic domain of VpU plays a central role in CD4 downregulation. We investigated structural consequences of phosphorylation of the two serines using nuclear magnetic resonance spectroscopy. A uniformly 15N and 13C stable isotope-labeled 45-residue peptide comprising the cytoplasmic domain of VpU (VpUcyt) was recombinantly produced in E .coli. The peptide forms two helices (commonly referred to as helix 2 and 3) in the presence of membrane mimicking dodecylphosphocholine (DPC) micelles, which flank a flexible region containing the two phosphorylation sites. Phosphorylation does not cause any drastic structural changes in the secondary structure of VpUcyt. However, an N-terminal elongation of helix 3 and a slightly reduced helicity at the C-terminus of helix 2 are observed upon phosphorylation based on characteristic changes of 13Calpha and 13Cbeta chemical shifts. Phosphorylation also reduces the local mobility of the protein backbone in the loop region containing the phosphorylation sites according to heteronuclear 1H--15N nuclear Overhauser enhancement (NOE) data.
000062891 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000062891 588__ $$aDataset connected to Web of Science, Pubmed
000062891 650_2 $$2MeSH$$aCytoplasm: chemistry
000062891 650_2 $$2MeSH$$aCytoplasm: metabolism
000062891 650_2 $$2MeSH$$aHIV-1: chemistry
000062891 650_2 $$2MeSH$$aHuman Immunodeficiency Virus Proteins: chemistry
000062891 650_2 $$2MeSH$$aHuman Immunodeficiency Virus Proteins: metabolism
000062891 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000062891 650_2 $$2MeSH$$aPhosphoserine: chemistry
000062891 650_2 $$2MeSH$$aPhosphoserine: metabolism
000062891 650_2 $$2MeSH$$aProtein Structure, Tertiary
000062891 650_2 $$2MeSH$$aViral Regulatory and Accessory Proteins: chemistry
000062891 650_2 $$2MeSH$$aViral Regulatory and Accessory Proteins: metabolism
000062891 650_7 $$00$$2NLM Chemicals$$aHuman Immunodeficiency Virus Proteins
000062891 650_7 $$00$$2NLM Chemicals$$aViral Regulatory and Accessory Proteins
000062891 650_7 $$00$$2NLM Chemicals$$avpu protein, Human immunodeficiency virus 1
000062891 650_7 $$017885-08-4$$2NLM Chemicals$$aPhosphoserine
000062891 650_7 $$2WoSType$$aJ
000062891 65320 $$2Author$$aHIV-1
000062891 65320 $$2Author$$aVpU
000062891 65320 $$2Author$$aCD4
000062891 65320 $$2Author$$aphosphorylation
000062891 65320 $$2Author$$aNMR
000062891 65320 $$2Author$$aviral accessory protein
000062891 7001_ $$0P:(DE-Juel1)132009$$aKoenig, B. W.$$b1$$uFZJ
000062891 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b2$$uFZJ
000062891 773__ $$0PERI:(DE-600)1491819-5$$a10.1002/psc.1004$$gVol. 14, p. 804 - 810$$p804 - 810$$q14<804 - 810$$tJournal of peptide science$$v14$$x1075-2617$$y2008
000062891 8567_ $$uhttp://dx.doi.org/10.1002/psc.1004
000062891 909CO $$ooai:juser.fz-juelich.de:62891$$pVDB
000062891 9131_ $$0G:(DE-Juel1)FUEK409$$bGesundheit$$kP33$$lFunktion und Dysfunktion des Nervensystems$$vFunktion und Dysfunktion des Nervensystems$$x0
000062891 9141_ $$y2008
000062891 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000062891 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
000062891 970__ $$aVDB:(DE-Juel1)99804
000062891 980__ $$aVDB
000062891 980__ $$aConvertedRecord
000062891 980__ $$ajournal
000062891 980__ $$aI:(DE-Juel1)ISB-2-20090406
000062891 980__ $$aUNRESTRICTED
000062891 980__ $$aI:(DE-Juel1)ICS-6-20110106
000062891 981__ $$aI:(DE-Juel1)IBI-7-20200312
000062891 981__ $$aI:(DE-Juel1)ISB-2-20090406
000062891 981__ $$aI:(DE-Juel1)ICS-6-20110106