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The Nipah virus phosphoprotein, P, is multimeric and tethers the viral polymerase to the nucleocapsid. We present the crystal structure of the multimerization domain of Nipah P: a long, parallel, tetrameric, coiled coil with a small, alpha-helical cap structure. Across the paramyxoviruses, these domains share little sequence identity; yet retain similar length and structural organization, suggesting a common requirement for scaffolding or spatial organization of the functions of P in the virus life cycle.

Crystal structure of the Nipah virus phosphoprotein tetramerization domain., Bruhn-Johannsen JF, Barnett K, Bibby J, Thomas J, Keegan R, Rigden D, Bornholdt ZA, Saphire EO, J Virol. 2013 Oct 23. PMID:24155387

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Barnett, K. | Bibby, J. | Bornholdt, Z A. | Bruhn, J F. | Keegan, R. | Rigden, D. | Saphire, E O. | Thomas, J. | Interferon inhibitor | Nucleoprotein chaperone | Viral polymerase co-factor | Viral protein