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

被引：97

作者：

Area, E ^{[1
]}

Martín-Benito, J ^{[1
]}

Gastaminza, P ^{[1
]}

Torreira, E ^{[1
]}

Valpuesta, JM ^{[1
]}

Carrascosa, JL ^{[1
]}

Ortín, J ^{[1
]}

机构：

[1] Ctr Nacl Biotecnol, E-28049 Madrid, Spain

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2004年 / 101卷 / 01期

关键词：

D O I：

10.1073/pnas.0307127101

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：308 / 313

页数：6

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