Structural models of the bovine papillomavirus E5 protein

Autor:	T, Surti, O, Klein, K, Aschheim, D, DiMaio, S O, Smith
Rok vydání:	1998
Předmět:	Models Molecular Receptor Platelet-Derived Growth Factor beta Kinetics Protein Conformation Spectroscopy Fourier Transform Infrared Animals Cattle Computer Simulation Receptors Platelet-Derived Growth Factor Oncogene Proteins Viral Dimerization Algorithms Protein Structure Secondary
Zdroj:	Proteins. 33(4)
ISSN:	0887-3585
Popis:	The bovine papillomavirus E5 protein is thought to be a type II integral membrane protein that exists as a disulfide-linked homodimer in transformed cells. Polarized-infrared measurements show that the E5 dimer in membrane bilayers is largely alpha-helical and has a transmembrane orientation. Computational searches of helix-helix conformations reveal two possible low-energy dimer structures. Correlation of these results with previous mutagenesis studies on the E5 protein suggests how the E5 dimer may serve as a molecular scaffold for dimerization and ligand-independent activation of the PDGF-beta receptor. We propose that on each face of the E5 dimer a PDGF-beta receptor molecule interacts directly with Gln17 from one E5 monomer and with Asp33 from the other E5 monomer. This model accounts for the requirement of Gln17 and Asp33 for complex formation and explains genetic results that dimerization of the E5 protein is essential for cell transformation.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::8034731d2776d83c038e80e9af74f1fa https://pubmed.ncbi.nlm.nih.gov/9849943 Zobrazit plný text záznamu Plný text