2ebo
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CORE STRUCTURE OF GP2 FROM EBOLA VIRUS
OverviewOverview
Ebola virions contain a surface transmembrane glycoprotein (GP) that is, responsible for binding to target cells and subsequent fusion of the viral, and host-cell membranes. GP is expressed as a single-chain precursor that, is posttranslationally processed into the disulfide-linked fragments GP1, and GP2. The GP2 subunit is thought to mediate membrane fusion. A soluble, fragment of the GP2 ectodomain, lacking the fusion-peptide region and the, transmembrane helix, folds into a stable, highly helical structure in, aqueous solution. Limited proteolysis studies identify a stable core of, the GP2 ectodomain. This 74-residue core, denoted Ebo-74, was, crystallized, and its x-ray structure was determined at 1.9-A resolution., Ebo-74 forms a trimer in which a long, central three-stranded coiled coil, is surrounded by shorter C-terminal helices that are packed in an, antiparallel orientation into hydrophobic grooves on the surface of the, coiled coil. Our results confirm the previously anticipated structural, similarity between the Ebola GP2 ectodomain and the core of the, transmembrane subunit from oncogenic retroviruses. The Ebo-74 structure, likely represents the fusion-active conformation of the protein, and its, overall architecture resembles several other viral membrane-fusion, proteins, including those from HIV and influenza.
About this StructureAbout this Structure
2EBO is a Single protein structure of sequence from Ebola virus sp. with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution., Malashkevich VN, Schneider BJ, McNally ML, Milhollen MA, Pang JX, Kim PS, Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2662-7. PMID:10077567
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