2gmo
From Proteopedia
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'''NMR-structure of an independently folded C-terminal domain of influenza polymerase subunit PB2''' | '''NMR-structure of an independently folded C-terminal domain of influenza polymerase subunit PB2''' | ||
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[[Category: Simorre, J P.]] | [[Category: Simorre, J P.]] | ||
[[Category: Tarendeau, F.]] | [[Category: Tarendeau, F.]] | ||
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Revision as of 02:16, 4 May 2008
NMR-structure of an independently folded C-terminal domain of influenza polymerase subunit PB2
Overview
The trimeric influenza virus polymerase, comprising subunits PA, PB1 and PB2, is responsible for transcription and replication of the segmented viral RNA genome. Using a novel library-based screening technique called expression of soluble proteins by random incremental truncation (ESPRIT), we identified an independently folded C-terminal domain from PB2 and determined its solution structure by NMR. Using green fluorescent protein fusions, we show that both the domain and the full-length PB2 subunit are efficiently imported into the nucleus dependent on a previously overlooked bipartite nuclear localization sequence (NLS). The crystal structure of the domain complexed with human importin alpha5 shows how the last 20 residues unfold to permit binding to the import factor. The domain contains three surface residues implicated in adaptation from avian to mammalian hosts. One of these tethers the NLS-containing peptide to the core of the domain in the unbound state.
About this Structure
2GMO is a Single protein structure of sequence from Influenza a virus. Full crystallographic information is available from OCA.
Reference
Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit., Tarendeau F, Boudet J, Guilligay D, Mas PJ, Bougault CM, Boulo S, Baudin F, Ruigrok RW, Daigle N, Ellenberg J, Cusack S, Simorre JP, Hart DJ, Nat Struct Mol Biol. 2007 Mar;14(3):229-33. Epub 2007 Feb 25. PMID:17310249 Page seeded by OCA on Sun May 4 05:16:42 2008
