6vkm

Crystal Structure of Stabilized GP from Makona Variant of Ebola Virus

spinqualitylabelsall models 6vkm, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Ebola virus causes severe hemorrhagic fever, often leading to death in humans. The trimeric fusion glycoprotein (GP) is the sole target for neutralizing antibodies and is the major focus of vaccine development. Soluble GP ectodomains are unstable and mostly monomeric when not fused to a heterologous trimerization domain. Here, we report structure-based designs of Ebola and Marburg GP trimers based on a stabilizing mutation in the hinge loop in refolding region 1 and substitution of a partially buried charge at the interface of the GP1 and GP2 subunits. The combined substitutions (T577P and K588F) substantially increased trimer expression for Ebola GP proteins. We determined the crystal structure of stabilized GP from the Makona Zaire ebolavirus strain without a trimerization domain or complexed ligand. The structure reveals that the stabilized GP adopts the same trimeric prefusion conformation, provides insight into triggering of GP conformational changes, and should inform future filovirus vaccine development. Structure-Based Design of Prefusion-Stabilized Filovirus Glycoprotein Trimers.,Rutten L, Gilman MSA, Blokland S, Juraszek J, McLellan JS, Langedijk JPM Cell Rep. 2020 Mar 31;30(13):4540-4550.e3. doi: 10.1016/j.celrep.2020.03.025. PMID:32234486 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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