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Literature DB >> 23576502

Structure of the tetramerization domain of measles virus phosphoprotein.

Guillaume Communie¹, Thibaut Crépin, Damien Maurin, Malene Ringkjøbing Jensen, Martin Blackledge, Rob W H Ruigrok.

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.

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Year: 2013 PMID： 23576502 PMCID： PMC3676081 DOI： 10.1128/JVI.00487-13

Source DB: PubMed Journal: J Virol ISSN： 0022-538X Impact factor: 5.103

27 in total

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6. Buried polar residues in coiled-coil interfaces.

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10. REFMAC5 for the refinement of macromolecular crystal structures.

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6. The C Protein Is Recruited to Measles Virus Ribonucleocapsids by the Phosphoprotein.

Authors: Christian K Pfaller; Louis-Marie Bloyet; Ryan C Donohue; Amanda L Huff; William P Bartemes; Iris Yousaf; Erica Urzua; Mathieu Clavière; Marie Zachary; Valentin de Masson d'Autume; Sandra Carson; Adam J Schieferecke; Alyssa J Meyer; Denis Gerlier; Roberto Cattaneo
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