5j81

Crystal structure of Glycoprotein C from Puumala virus in the post-fusion conformation (pH 6.0)

spinqualitylabelsall models 5j81, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5j81 is a 1 chain structure with sequence from Puumala virus p360. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: ACT, BMA, NAG, P33, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GP_PUUMP Glycoprotein N and Glycoprotein C interact with each other and are present at the surface of the virion. They are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Also promote fusion of viral membrane with host endosomal membrane after endocytosis of the virion. Glycoprotein N contains an ITAM motif which is likely to dysregulate normal immune and endothelial cell responses and contribute to virus pathogenesis (By similarity). Publication Abstract from PubMed Hantaviruses are important emerging human pathogens and are the causative agents of serious diseases in humans with high mortality rates. Like other members in the Bunyaviridae family their M segment encodes two glycoproteins, GN and GC, which are responsible for the early events of infection. Hantaviruses deliver their tripartite genome into the cytoplasm by fusion of the viral and endosomal membranes in response to the reduced pH of the endosome. Unlike phleboviruses (e.g. Rift valley fever virus), that have an icosahedral glycoprotein envelope, hantaviruses display a pleomorphic virion morphology as GN and GC assemble into spikes with apparent four-fold symmetry organized in a grid-like pattern on the viral membrane. Here we present the crystal structure of glycoprotein C (GC) from Puumala virus (PUUV), a representative member of the Hantavirus genus. The crystal structure shows GC as the membrane fusion effector of PUUV and it presents a class II membrane fusion protein fold. Furthermore, GC was crystallized in its post-fusion trimeric conformation that until now had been observed only in Flavi- and Togaviridae family members. The PUUV GC structure together with our functional data provides intriguing evolutionary and mechanistic insights into class II membrane fusion proteins and reveals new targets for membrane fusion inhibitors against these important pathogens. Crystal Structure of Glycoprotein C from a Hantavirus in the Post-fusion Conformation.,Willensky S, Bar-Rogovsky H, Bignon EA, Tischler ND, Modis Y, Dessau M PLoS Pathog. 2016 Oct 26;12(10):e1005948. doi: 10.1371/journal.ppat.1005948., eCollection 2016 Oct. PMID:27783673 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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