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The Structural Basis for an Essential Subunit Interaction in Influenza Virus RNA Polymerase.

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  • インフルエンザウイルスのRNAポリメラーゼPA‐PB1複合体のX線結晶構造解析
  • インフルエンザウイルスのRNAポリメラーゼPA-PB1複合体のX線結晶構造解析
  • インフルエンザウイルス ノ RNA ポリメラーゼ PA PB1 フクゴウタイ ノ Xセン ケッショウ コウゾウ カイセキ

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Abstract

Influenza A virus is a major human and animal pathogen with the potential to cause catastrophic loss of life. The virus reproduces rapidly, mutates frequently, and occasionally crosses species barriers. The recent emergence in Asia of avian influenza related to highly pathogenic forms of the human virus has highlighted the urgent need for new effective treatments. No current medication targets this heterotrimeric polymerase complex. All three subunits, PB1, PB2, and PA are required for both transcription and replication. PB1 carries the polymerise active site, PB2 includes the capped-RNA recognition domain, and PA is involved in assembly of the functional complex, but so far very little structural information has been reported for any of them. We describe the crystal structure of a large fragment of one subunit (PA) of influenza A RNA polymerise bound to a fragment of another subunit (PB1) . The C terminal domain of PA forms a novel fold, and forms a deep, highly hydrophobic groove into which the N-terminal residues of PB1 can fit by forming a 310 helix.

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