3oa9

Effector domain of influenza A/Duck/Albany/76 NS1

spinqualitylabelsall models 3oa9, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3oa9 is a 2 chain structure with sequence from Influenza a virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3d6r, 3o9q, 3o9r, 3o9s, 3o9t, 3o9u Gene: NS (Influenza A virus) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Influenza A virus NS1 protein is a multifunctional virulence factor consisting of an RNA binding domain (RBD), a short linker, an effector domain (ED), and a C-terminal 'tail'. Although poorly understood, NS1 multimerization may autoregulate its actions. While RBD dimerization seems functionally conserved, two possible apo ED dimers have been proposed (helix-helix and strand-strand). Here, we analyze all available RBD, ED, and full-length NS1 structures, including four novel crystal structures obtained using EDs from divergent human and avian viruses, as well as two forms of a monomeric ED mutant. The data reveal the helix-helix interface as the only strictly conserved ED homodimeric contact. Furthermore, a mutant NS1 unable to form the helix-helix dimer is compromised in its ability to bind dsRNA efficiently, implying that ED multimerization influences RBD activity. Our bioinformatical work also suggests that the helix-helix interface is variable and transient, thereby allowing two ED monomers to twist relative to one another and possibly separate. In this regard, we found a mAb that recognizes NS1 via a residue completely buried within the ED helix-helix interface, and which may help highlight potential different conformational populations of NS1 (putatively termed 'helix-closed' and 'helix-open') in virus-infected cells. 'Helix-closed' conformations appear to enhance dsRNA binding, and 'helix-open' conformations allow otherwise inaccessible interactions with host factors. Our data support a new model of NS1 regulation in which the RBD remains dimeric throughout infection, while the ED switches between several quaternary states in order to expand its functional space. Such a concept may be applicable to other small multifunctional proteins. A Transient Homotypic Interaction Model for the Influenza A Virus NS1 Protein Effector Domain.,Kerry PS, Ayllon J, Taylor MA, Hass C, Lewis A, Garcia-Sastre A, Randall RE, Hale BG, Russell RJ PLoS One. 2011 Mar 28;6(3):e17946. PMID:21464929 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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