| Literature DB >> 14691253 |
Estela Area1, Jaime Martín-Benito, Pablo Gastaminza, Eva Torreira, José M Valpuesta, José L Carrascosa, Juan Ortín.
Abstract
The 3D structure of the influenza virus polymerase complex was determined by electron microscopy and image processing of recombinant ribonucleoproteins (RNPs). The RNPs were generated by in vivo amplification using cDNAs of the three polymerase subunits, the nucleoprotein, and a model virus-associated RNA containing 248 nt. The polymerase structure obtained is very compact, with no apparent boundaries among subunits. The position of specific regions of the PB1, PB2, and PA subunits was determined by 3D reconstruction of either RNP-mAb complexes or tagged RNPs. This structural model is available for the polymerase of a negative-stranded RNA virus and provides a general delineation of the complex and its interaction with the template-associated nucleoprotein monomers in the RNP.Entities:
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Year: 2003 PMID: 14691253 PMCID: PMC314181 DOI: 10.1073/pnas.0307127101
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205