dc.contributor.author
Olal, Daniel
dc.contributor.author
Daumke, Oliver
dc.date.accessioned
2018-06-08T07:16:46Z
dc.date.available
2016-04-07T08:06:04.255Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/17567
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-21451
dc.description.abstract
Hantaviruses are etiological agents of life-threatening hemorrhagic fever with
renal syndrome and hantavirus cardiopulmonary syndrome. The nucleoprotein (N)
of hantavirus is essential for viral transcription and replication, thus
representing an attractive target for therapeutic intervention. We have
determined the crystal structure of hantavirus N to 3.2 Å resolution. The
structure reveals a two-lobed, mostly α-helical structure that is distantly
related to that of orthobunyavirus Ns. A basic RNA binding pocket is located
at the intersection between the two lobes. We provide evidence that
oligomerization is mediated by amino- and C-terminal arms that bind to the
adjacent monomers. Based on these findings, we suggest a model for the
oligomeric ribonucleoprotein (RNP) complex. Our structure provides mechanistic
insights into RNA encapsidation in the genus Hantavirus and constitutes a
template for drug discovery efforts aimed at combating hantavirus infections.
en
dc.rights.uri
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::572 Biochemie
dc.title
Structure of the Hantavirus Nucleoprotein Provides Insights into the Mechanism
of RNA Encapsidation
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Cell Reports. - 14 (2016), 9, S. 2092-2099
dcterms.bibliographicCitation.doi
10.1016/j.celrep.2016.02.005
dcterms.bibliographicCitation.url
http://www.sciencedirect.com/science/article/pii/S2211124716300730
refubium.affiliation
Biologie, Chemie, Pharmazie
de
refubium.mycore.fudocsId
FUDOCS_document_000000024333
refubium.note.author
Der Artikel wurde in einer Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000006250
dcterms.accessRights.openaire
open access