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000007147 0247_ $$2DOI$$a10.1016/j.bbamem.2009.09.010
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000007147 084__ $$2WoS$$aBiochemistry & Molecular Biology
000007147 084__ $$2WoS$$aBiophysics
000007147 1001_ $$0P:(DE-Juel1)VDB28257$$aWittlich, M.$$b0$$uFZJ
000007147 245__ $$aNMR structure of the transmembrane and cytoplasmic domains of human CD4 in micelles
000007147 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2010
000007147 300__ $$a122 - 127
000007147 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000007147 440_0 $$0802$$aBiochimica et Biophysica Acta$$v1798$$x0006-3002$$y2
000007147 500__ $$aThis work has been supported by a grant from the "Prasidentenfond der Helmholtzgemeinschaft" (HGF, "Virtual Institute of Structural Biology") to D.W.
000007147 520__ $$aThe human cluster determinant 4 (CD4) is a type I transmembrane glycoprotein involved in T-cell signalling. It is expressed primarily on the surface of T helper cells but also on subsets of memory and regulatory T lymphocytes (CD4(+) cells). It serves as a coreceptor in T-cell receptor recognition of MHC II antigen complexes. Besides its cellular functions, CD4 serves as the main receptor for human immunodeficiency virus type I (HIV-1). During T-cell infection, the CD4 extracellular domain is bound by HIV-1 gp120, the viral surface glycoprotein, which triggers a number of conformational changes ultimately resulting in virion entry of the cell. Subsequently, CD4 is downregulated in infected cells by multiple strategies that involve direct interactions of the HIV-1 proteins VpU and Nef with the cytoplasmic part of CD4. In the present work, we describe the NOE-based solution structure of the transmembrane and cytoplasmic domains of the cystein-free variant of CD4 (CD4mut) in dodecylphosphocholine (DPC) micelles. Furthermore, we have characterized micelle-inserted CD4mut by paramagentic relaxation enhancement (PRE) agents and (1)H-(15)N heteronuclear NOE data. CD4mut features a stable and well-defined transmembrane helix from M372 to V395 buried in the micellar core and a cytoplasmic helix ranging from A404 to L413. Experimental data suggest the amphipathic cytoplasmic helix to be in close contact with the micellar surface. The role of the amphipathic helix and its interaction with the micellar surface is discussed with respect to the biological function of the full-length CD4 protein.
000007147 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000007147 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000007147 588__ $$aDataset connected to Web of Science, Pubmed
000007147 650_2 $$2MeSH$$aAntigens, CD4: chemistry
000007147 650_2 $$2MeSH$$aAntigens, CD4: immunology
000007147 650_2 $$2MeSH$$aAntigens, CD4: metabolism
000007147 650_2 $$2MeSH$$aHumans
000007147 650_2 $$2MeSH$$aMicelles
000007147 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular: methods
000007147 650_2 $$2MeSH$$aPhosphorylcholine: analogs & derivatives
000007147 650_2 $$2MeSH$$aPhosphorylcholine: chemistry
000007147 650_2 $$2MeSH$$aPhosphorylcholine: metabolism
000007147 650_2 $$2MeSH$$aProtein Structure, Secondary: physiology
000007147 650_2 $$2MeSH$$aProtein Structure, Tertiary: physiology
000007147 650_7 $$00$$2NLM Chemicals$$aAntigens, CD4
000007147 650_7 $$00$$2NLM Chemicals$$aMicelles
000007147 650_7 $$0107-73-3$$2NLM Chemicals$$aPhosphorylcholine
000007147 650_7 $$053949-18-1$$2NLM Chemicals$$adodecylphosphocholine
000007147 650_7 $$2WoSType$$aJ
000007147 65320 $$2Author$$aCD4
000007147 65320 $$2Author$$aHIV-1
000007147 65320 $$2Author$$aVpU
000007147 65320 $$2Author$$aMembrane protein
000007147 65320 $$2Author$$aNMR
000007147 7001_ $$0P:(DE-Juel1)VDB89240$$aThiagarajan, P.$$b1$$uFZJ
000007147 7001_ $$0P:(DE-Juel1)132009$$aKoenig, B. W.$$b2$$uFZJ
000007147 7001_ $$0P:(DE-Juel1)VDB57647$$aHartmann, R.$$b3$$uFZJ
000007147 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000007147 773__ $$0PERI:(DE-600)1460387-1$$a10.1016/j.bbamem.2009.09.010$$gVol. 1798, p. 122 - 127$$p122 - 127$$q1798<122 - 127$$tBiochimica et biophysica acta$$v1798$$x0006-3002$$y2010
000007147 8567_ $$uhttp://dx.doi.org/10.1016/j.bbamem.2009.09.010
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