The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein

Journal of Biological Chemistry

Volumn 278, Issue 20, 2003, Pages 18638-18648

  Longhi, Sonia ^a,d   Receveur Bréchot, Véronique ^a   Karlin, David ^a   Johansson, Kenth ^a   Darbon, Hervé ^a   Bhella, David ^b   Yeo, Robert ^b   Finet, Stéphanie ^c   Canard, Bruno ^a  

^a AIX MARSEILLE UNIVERSITY   (France)

^b INSTITUTE OF VIROLOGY   (United Kingdom)

^c EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^d CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BINDING ENERGY; CONFORMATIONS; HYDRODYNAMICS; LIGHT SCATTERING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; VIRUSES; X RAY SCATTERING;

PROTEOLYSIS;

BIOCHEMICAL ENGINEERING;

PHOSPHOPROTEIN; VIRUS NUCLEOPROTEIN; EPITOPE; NUCLEOPROTEIN; NUCLEOPROTEIN, MEASLES VIRUS; VIRUS PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ELECTRON MICROSCOPY; GEL FILTRATION; HYDRODYNAMICS; LIGHT SCATTERING; MEASLES VIRUS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STRUCTURE; VIRUS NUCLEOCAPSID; X RAY CRYSTALLOGRAPHY; CHEMISTRY; ESCHERICHIA COLI; GEL CHROMATOGRAPHY; LIGHT; MASS SPECTROMETRY; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PLASMID; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RADIATION SCATTERING; SERODIAGNOSIS; X RAY;

BACTERIA (MICROORGANISMS); MEASLES VIRUS; RNA VIRUSES;

CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; EPITOPES; ESCHERICHIA COLI; LIGHT; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; NUCLEOPROTEINS; PLASMIDS; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SCATTERING, RADIATION; VIRAL PROTEINS; X-RAYS;

EID: 0037705413     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M300518200     Document Type: Article

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