Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7. 2006

O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
Fritz-Lipmann-Institut, Jena, Germany.

The oncoprotein E7 of human papilloma viruses (HPV) is involved in the pathogenesis and maintenance of human cervical cancers. The most prevalent HPV types found in cervix carcinomas are HPV16, 18 and 45. The structure of the E7 dimer from HPV45 (PDB 2F8B) was determined by nuclear magnetic resonance spectroscopy. Each monomer comprises an unfolded N-terminus and a well-structured C-terminal domain with a beta1beta2alpha1beta3alpha2 topology representing a unique zinc-binding fold found only for E7. Dimerization occurs through the alpha1/alpha1' helices and intermolecular beta-sheet formation but excludes the zinc-binding sites. E7 is reported to interact with a number of cellular proteins (e.g. pRb, p21(CIP1)). Binding of a peptide derived from the C-terminus of p21(CIP1) to the C-terminal domain of E7 was characterized by monitoring chemical shift perturbations of the amide groups of E7. This provides direct evidence that a shallow groove situated between alpha1 and beta1 of the E7 C-terminal domain is interacting with the C-terminus of p21(CIP1). Intriguingly, this binding site overlaps with the low-affinity binding site on E7 for the C-domain of pRb.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D009856 Oncogene Proteins, Viral Products of viral oncogenes, most commonly retroviral oncogenes. They usually have transforming and often protein kinase activities. Viral Oncogene Proteins,Viral Transforming Proteins,v-onc Proteins,Transforming Proteins, Viral,v onc Proteins
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D012307 Risk Factors An aspect of personal behavior or lifestyle, environmental exposure, inborn or inherited characteristic, which, based on epidemiological evidence, is known to be associated with a health-related condition considered important to prevent. Health Correlates,Risk Factor Scores,Risk Scores,Social Risk Factors,Population at Risk,Populations at Risk,Correlates, Health,Factor, Risk,Factor, Social Risk,Factors, Social Risk,Risk Factor,Risk Factor Score,Risk Factor, Social,Risk Factors, Social,Risk Score,Score, Risk,Score, Risk Factor,Social Risk Factor
D012996 Solutions The homogeneous mixtures formed by the mixing of a solid, liquid, or gaseous substance (solute) with a liquid (the solvent), from which the dissolved substances can be recovered by physical processes. (From Grant & Hackh's Chemical Dictionary, 5th ed) Solution
D016335 Zinc Fingers Motifs in DNA- and RNA-binding proteins whose amino acids are folded into a single structural unit around a zinc atom. In the classic zinc finger, one zinc atom is bound to two cysteines and two histidines. In between the cysteines and histidines are 12 residues which form a DNA binding fingertip. By variations in the composition of the sequences in the fingertip and the number and spacing of tandem repeats of the motif, zinc fingers can form a large number of different sequence specific binding sites. Zinc Finger DNA-Binding Domains,Zinc Finger Motifs,Finger, Zinc,Fingers, Zinc,Motif, Zinc Finger,Motifs, Zinc Finger,Zinc Finger,Zinc Finger DNA Binding Domains,Zinc Finger Motif
D017510 Protein Folding Processes involved in the formation of TERTIARY PROTEIN STRUCTURE. Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D050725 Papillomavirus E7 Proteins ONCOGENE PROTEINS from papillomavirus that deregulate the CELL CYCLE of infected cells and lead to NEOPLASTIC CELL TRANSFORMATION. Papillomavirus E7 proteins have been shown to interact with various regulators of the cell cycle including RETINOBLASTOMA PROTEIN and certain cyclin-dependent kinase inhibitors. E7 Oncogene Proteins,Oncogene Protein E7, Papillomavirus,E7 Proteins, Papillomavirus,Oncogene Proteins, E7

Related Publications

O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
June 2017, Scientific reports,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
February 1989, Science (New York, N.Y.),
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
December 2007, Clinical cancer research : an official journal of the American Association for Cancer Research,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
February 2009, Virology,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
January 2021, Frontiers in immunology,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
January 2011, International journal of immunopathology and pharmacology,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
April 1992, Journal of virology,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
June 2003, Vaccine,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
April 1998, Journal of biomolecular NMR,
O Ohlenschläger, and T Seiboth, and H Zengerling, and L Briese, and A Marchanka, and R Ramachandran, and M Baum, and M Korbas, and W Meyer-Klaucke, and M Dürst, and M Görlach
December 2020, Proteins,
Copied contents to your clipboard!