title: Crystal structure of the nipah virus phosphoprotein tetramerization domain.
abstract: 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 virus P: a long, parallel, tetrameric, coiled coil with a small, α-helical cap structure. Across the paramyxoviruses, these domains share little sequence identity yet are similar in length and structural organization, suggesting a common requirement for scaffolding or spatial organization of the functions of P in the virus life cycle.
authors.affiliation: Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
authors.forename: Jessica F
authors.initials: JF
authors.lastname: Bruhn
authors.forename: Katherine C
authors.initials: KC
authors.lastname: Barnett
authors.forename: Jaclyn
authors.initials: J
authors.lastname: Bibby
authors.forename: Jens M H
authors.initials: JM
authors.lastname: Thomas
authors.forename: Ronan M
authors.initials: RM
authors.lastname: Keegan
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Rigden
authors.forename: Zachary A
authors.initials: ZA
authors.lastname: Bornholdt
authors.forename: Erica Ollmann
authors.initials: EO
authors.lastname: Saphire
mesh_terms: D001704:Biopolymers / Q000737:chemistry*; D018360:Crystallography, X-Ray; D045405:Nipah Virus / Q000737:chemistry*; D010750:Phosphoproteins / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D001704:Biopolymers; D010750:Phosphoproteins