7zny

Cryo-EM structure of the canine distemper virus tetrameric attachment glycoprotein

spinqualitylabelsall models 7zny, resolution 3.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7zny is a 4 chain structure with sequence from Morbillivirus canis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.26Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9QPQ8_9MONO Publication Abstract from PubMed Canine distemper virus (CDV) is an enveloped RNA morbillivirus that triggers respiratory, enteric, and high incidence of severe neurological disorders. CDV induces devastating outbreaks in wild and endangered animals as well as in domestic dogs in countries associated with suboptimal vaccination programs. The receptor-binding tetrameric attachment (H)-protein is part of the morbilliviral cell entry machinery. Here, we present the cryo-electron microscopy (cryo-EM) structure and supramolecular organization of the tetrameric CDV H-protein ectodomain. The structure reveals that the morbilliviral H-protein is composed of three main domains: stalk, neck, and heads. The most unexpected feature was the inherent asymmetric architecture of the CDV H-tetramer being shaped by the neck, which folds into an almost 90 degrees bent conformation with respect to the stalk. Consequently, two non-contacting receptor-binding H-head dimers, which are also tilted toward each other, are located on one side of an intertwined four helical bundle stalk domain. Positioning of the four protomer polypeptide chains within the neck domain is guided by a glycine residue (G158), which forms a hinge point exclusively in two protomer polypeptide chains. Molecular dynamics simulations validated the stability of the asymmetric structure under near physiological conditions and molecular docking showed that two receptor-binding sites are fully accessible. Thus, this spatial organization of the CDV H-tetramer would allow for concomitant protein interactions with the stalk and head domains without steric clashes. In summary, the structure of the CDV H-protein ectodomain provides new insights into the morbilliviral cell entry system and offers a blueprint for next-generation structure-based antiviral drug discovery. Structure and supramolecular organization of the canine distemper virus attachment glycoprotein.,Kalbermatter D, Jeckelmann JM, Wyss M, Shrestha N, Pliatsika D, Riedl R, Lemmin T, Plattet P, Fotiadis D Proc Natl Acad Sci U S A. 2023 Feb 7;120(6):e2208866120. doi: , 10.1073/pnas.2208866120. Epub 2023 Jan 30. PMID:36716368 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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