Structural highlights
Function
D2DEB8_NIPAV
Publication Abstract from PubMed
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bruhn-Johannsen JF, Barnett K, Bibby J, Thomas J, Keegan R, Rigden D, Bornholdt ZA, Saphire EO. Crystal structure of the Nipah virus phosphoprotein tetramerization domain. J Virol. 2013 Oct 23. PMID:24155387 doi:http://dx.doi.org/10.1128/JVI.02294-13