2wfo | pdb_00002wfo

Crystal structure of Machupo virus envelope glycoprotein GP1

spinqualitylabelsall models 2wfo, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wfo is a 1 chain structure with sequence from Machu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. This first structure of an arenavirus glycoprotein shows that GP1 consists of a novel alpha/beta fold. This provides a blueprint of the New World arenavirus attachment glycoproteins and reveals a new architecture of viral attachment, using a protein fold of unknown origins. Unusual molecular architecture of the machupo virus attachment glycoprotein.,Bowden TA, Crispin M, Graham SC, Harvey DJ, Grimes JM, Jones EY, Stuart DI J Virol. 2009 Aug;83(16):8259-65. Epub 2009 Jun 3. PMID:19494008 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycoprotein GP 3D structures

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