Structure of the Tetramerization Domain of Measles Virus Phosphoprotein-Reference-Cited by-同舟云学术

Structure of the Tetramerization Domain of Measles Virus Phosphoprotein

Published:2013-06-15 Issue:12 Volume:87 Page:7166-7169
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Communie Guillaume¹²,Crépin Thibaut¹,Maurin Damien²,Jensen Malene Ringkjøbing²,Blackledge Martin²,Ruigrok Rob W. H.¹

Affiliation:

1. UJF-EMBL-CNRS, UMI 3265, Unit for Virus Host Cell Interactions, Grenoble, France

2. CEA-CNRS-UJF, UMR 5075, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France

Abstract

ABSTRACT The atomic structure of the stable tetramerization domain of the measles virus phosphoprotein shows a tight four-stranded coiled coil. Although at first sight similar to the tetramerization domain of the Sendai virus phosphoprotein, which has a hydrophilic interface, the measles virus domain has kinked helices that have a strongly hydrophobic interface and it lacks the additional N-terminal three helical bundles linking the long helices.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JVI.00487-13

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