The structural basis for an essential subunit interaction in influenza virus RNA polymerase

Eiji Obayashi, Hisashi Yoshida, Fumihiro Kawai, Naoya Shibayama, Atsushi Kawaguchi, Kyosuke Nagata, Jeremy R. H. Tame and Sam-Yong Park ()
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Eiji Obayashi: Protein Design Laboratory, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan
Hisashi Yoshida: Protein Design Laboratory, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan
Fumihiro Kawai: Protein Design Laboratory, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan
Naoya Shibayama: Jichi Medical University, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan
Atsushi Kawaguchi: Graduate School of Comprehensive Human Sciences and Institute of Basic Medical Sciences, University of Tsukuba
Kyosuke Nagata: Graduate School of Comprehensive Human Sciences and Institute of Basic Medical Sciences, University of Tsukuba
Jeremy R. H. Tame: Protein Design Laboratory, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan
Sam-Yong Park: Protein Design Laboratory, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama 230-0045, Japan

Nature, 2008, vol. 454, issue 7208, 1127-1131

Abstract: Influenza virus: polymerase structures determined Influenza A virus polymerase consists of three proteins, PA, PB1 and PB2, and is critical for transcription and replication. Two groups now report the crystal structure of the avian H5N1 PA C-terminal domain in complex with the PA binding domain of PB1. The structure work may be useful for the design of novel antiviral drugs.

Date: 2008
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DOI: 10.1038/nature07225

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