2ebo
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Ebola virions contain a surface transmembrane glycoprotein (GP) that is | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Ebola virus sp.]] | [[Category: Ebola virus sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
| - | [[Category: Malashkevich, V | + | [[Category: Malashkevich, V N.]] |
| - | [[Category: Mcnally, M | + | [[Category: Mcnally, M L.]] |
| - | [[Category: Milhollen, M | + | [[Category: Milhollen, M A.]] |
| - | [[Category: Pang, J | + | [[Category: Pang, J X.]] |
| - | [[Category: Schneider, B | + | [[Category: Schneider, B J.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: coat protein]] | [[Category: coat protein]] | ||
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[[Category: gp2]] | [[Category: gp2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:08:24 2008'' |
Revision as of 15:08, 21 February 2008
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CORE STRUCTURE OF GP2 FROM EBOLA VIRUS
Overview
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 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.
Reference
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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