3D structure of the influenza virus polymerase complex: Localization of subunit domains

@article{citeulike:2773912, 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. 10.1073/pnas.0307127101}, author = {Area, Estela and Martin-Benito, Jaime and Gastaminza, Pablo and Torreira, Eva and Valpuesta, Jose M. and Carrascosa, Jose L. and Ortin, Juan }, citeulike-article-id = {2773912}, doi = {10.1073/pnas.0307127101}, journal = {Proceedings of the National Academy of Sciences}, keywords = {complex, influenza, structure}, month = {January}, number = {1}, pages = {308--313}, posted-at = {2008-05-09 02:38:39}, priority = {2}, title = {3D structure of the influenza virus polymerase complex: Localization of subunit domains}, url = {http://dx.doi.org/10.1073/pnas.0307127101}, volume = {101}, year = {2004} }

TY - JOUR ID - citeulike:2773912 L3 - citeulike-article-id:2773912 TI - 3D structure of the influenza virus polymerase complex: Localization of subunit domains JF - Proceedings of the National Academy of Sciences VL - 101 IS - 1 SP - 308 EP - 313 N2 - 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. 10.1073/pnas.0307127101 KW - complex KW - influenza KW - structure AU - Area, Estela AU - Martin-Benito, Jaime AU - Gastaminza, Pablo AU - Torreira, Eva AU - Valpuesta, Jose AU - Carrascosa, Jose AU - Ortin, Juan PY - 2004/01/06/ UR - http://dx.doi.org/10.1073/pnas.0307127101 ER -