4n53

Human enterovirus 71 uncoating intermediate captured at atomic resolution

spinqualitylabelsall models 4n53, resolution 3.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n53 is a 4 chain structure with sequence from Enterovirus A71. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3063Å Ligands: SPH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function S5QA87_HE71 Publication Abstract from PubMed Human enterovirus 71 (EV71) is the major causative agent of severe hand-foot-and-mouth diseases (HFMD) in young children, and structural characterization of EV71 during its lifecycle can aid in the development of therapeutics against HFMD. Here, we present the atomic structures of the full virion and an uncoating intermediate of a clinical EV71 C4 strain to illustrate the structural changes in the full virion that lead to the formation of the uncoating intermediate prepared for RNA release. Although the VP1 N-terminal regions, observed to penetrate through the junction channel at the quasi 3-fold axis in the uncoating intermediate of coxsackievirus A16, were not observed in the EV71 uncoating intermediate, drastic conformational changes occur in this region, as has been observed in all capsid proteins. Additionally, the RNA genome interacts with the N-terminal extensions of VP1 and residues 32-36 of VP3, both of which are situated at the bottom of the junction. These observations highlight the importance of the junction for genome release. Furthermore, EV71 uncoating is associated with apparent rearrangements and expansion around the 2- and 5-fold axes without obvious changes around the 3-fold axes. Therefore, these structures enabled the identification of hot spots for capsid rearrangements, which led to the hypothesis that the protomer interface near the junction and the 2-fold axis permits the opening of large channels for the exit of polypeptides and viral RNA, which is an uncoating mechanism that is likely conserved in enteroviruses. Human Enterovirus 71 Uncoating Captured at Atomic Resolution.,Lyu K, Ding J, Han JF, Zhang Y, Wu XY, He YL, Qin CF, Chen R J Virol. 2013 Dec 18. PMID:24352461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat proteins 3D structures

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