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Solid-state 15N- and 19F-NMR analysis of the interaction of the viral E5 oncoprotein with the PDGF receptor in membranes

Grage, Stephan ORCID iD icon; Windisch, Dirk; Xu, Xiaojun; Ziegler, Colin; Wadhwani, Parvesh; Ulrich, Anne

Abstract (englisch):

The platelet-derived growth factor receptor (PDGFR) is a receptor tyrosine kinase that gets constitutively activated by the oncogenic E5 protein from papillomavirus, leading to uncontrolled proliferation and cancer. Bovine E5 with a length of only 44 amino acids consists largely of a transmembrane helix that can engage in specific helix-helix interactions with the transmembrane segment of PDGFR [1,2].
Our aim was to elucidate the structural criteria by which these transmembrane segments recognize each other and to describe the oligomeric bundle formed in the membrane. We used solid-state 15N-NMR to characterize the structure and alignment of E5 and PDGFR in lipid bilayers, each one alone and together in the hetero-oligomeric complex. When reconstituted alone in lipid bilayers, we observed that the E5 helix is inserted almost upright in thick membranes, but it starts to tilt and gets slightly deformed in moderately thinner bilayers, and it becomes aggregated in very thin membranes due to hydrophobic mismatch [3]. On the other hand, when reconstituted together with the receptor, E5 can compensate for the hydrophobic mismatch by binding to the transmembrane segment of the receptor. ... mehr

Zugehörige Institution(en) am KIT Institut für Biologische Grenzflächen (IBG)
Publikationstyp Vortrag
Publikationsjahr 2016
Sprache Englisch
Identifikator KITopen-ID: 1000061923
HGF-Programm 47.02.02 (POF III, LK 01) Zellpopul.auf Biofunk.Oberflächen IBG-2
Veranstaltung 27th International Conference on Magnetic Resonance in Biological Systems, 21-26.08.2016, Kyoto
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