4l3n

Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus

spinqualitylabelsall models 4l3n, resolution 2.13Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4l3n is a 2 chain structure with sequence from Human betacoronavirus 2c Jordan-N3/2012. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.13Å Ligands: EDO, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M4SVE7_MERS Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099] Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] Spike protein S2: mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Publication Abstract from PubMed The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people with a fatality rate of more than 50%. Alarmingly, the virus demonstrates a capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents the structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans. Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.,Chen Y, Rajashankar KR, Yang Y, Agnihothram SS, Liu C, Lin YL, Baric RS, Li F J Virol. 2013 Jul 31. PMID:23903833 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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