related to degree

• Bruhn, Jessica, Ph.D. in Biophysics, Scripps Research 2011 - 2016

authors

• Bruhn, Jessica
• Barnett, K. C.
• Bibby, J.
• Thomas, J. M. H.
• Keegan, R. M.
• Rigden, D. J.
• Bornholdt, Zachary
• Saphire, Erica Ollmann

publication date

• January 2014

journal

• Journal of Virology  Journal

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.

subject areas

• Biopolymers
• Crystallography, X-Ray
• Nipah Virus
• Phosphoproteins
• Protein Conformation

PubMed Central ID

• PMC3911761

International Standard Serial Number (ISSN)

• 0022-538X

Digital Object Identifier (DOI)

• 10.1128/jvi.02294-13

PubMed ID

• 24155387

start page

• 758

end page

• 762

volume

• 88

issue

• 1