7oa4

Crystal structure of the N-terminal endonuclease domain of La Crosse virus L-protein bound to compound L-742,001

spinqualitylabelsall models 7oa4, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7oa4 is a 4 chain structure with sequence from La Crosse virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: 0N8, FMT, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L_BUNLC Publication Abstract from PubMed The large Bunyavirales order includes several families of viruses with a segmented ambisense (-) RNA genome and a cytoplasmic life cycle that starts by synthesizing viral mRNA. The initiation of transcription, which is common to all members, relies on an endonuclease activity that is responsible for cap-snatching. In La Crosse virus, an orthobunyavirus, it has previously been shown that the cap-snatching endonuclease resides in the N-terminal domain of the L protein. Orthobunyaviruses are transmitted by arthropods and cause diseases in cattle. However, California encephalitis virus, La Crosse virus and Jamestown Canyon virus are North American species that can cause encephalitis in humans. No vaccines or antiviral drugs are available. In this study, three known Influenza virus endonuclease inhibitors (DPBA, L-742,001 and baloxavir) were repurposed on the La Crosse virus endonuclease. Their inhibition was evaluated by fluorescence resonance energy transfer and their mode of binding was then assessed by differential scanning fluorimetry and microscale thermophoresis. Finally, two crystallographic structures were obtained in complex with L-742,001 and baloxavir, providing access to the structural determinants of inhibition and offering key information for the further development of Bunyavirales endonuclease inhibitors. Biophysical and structural study of La Crosse virus endonuclease inhibition for the development of new antiviral options.,Feracci M, Hernandez S, Garlatti L, Mondielli C, Vincentelli R, Canard B, Reguera J, Ferron F, Alvarez K IUCrJ. 2024 May 1;11(Pt 3):374-383. doi: 10.1107/S205225252400304X. PMID:38656310 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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