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CRYSTAL STRUCTURE OF THE EBOLA VIRUS MEMBRANE-FUSION SUBUNIT, GP2, FROM THE ENVELOPE GLYCOPROTEIN ECTODOMAINCRYSTAL STRUCTURE OF THE EBOLA VIRUS MEMBRANE-FUSION SUBUNIT, GP2, FROM THE ENVELOPE GLYCOPROTEIN ECTODOMAIN
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the structure of GP2 from the Ebola virus membrane fusion glycoprotein by X-ray crystallography. The molecule contains a central triple-stranded coiled coil followed by a disulfide-bonded loop homologous to an immunosuppressive sequence in retroviral glycoproteins, which reverses the chain direction and connects to an alpha helix packed antiparallel to the core helices. The structure suggests that fusion peptides near the N termini form disulfide-bonded loops at one end of the molecule and that the C-terminal membrane anchors are at the same end. In this conformation, GP2 could both bridge two membranes and facilitate their apposition to initiate membrane fusion. We also find a heptad irregularity like that in low-pH-induced influenza HA2 and a solvent ion trapped in a coiled coil like that in retroviral TMs. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain.,Weissenhorn W, Carfi A, Lee KH, Skehel JJ, Wiley DC Mol Cell. 1998 Nov;2(5):605-16. PMID:9844633[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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