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Structure and dynam...
Structure and dynamics of membrane-associated ICP47, a viral inhibitor of the MHC I antigen-processing machinery
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- Aisenbrey, Christopher (författare)
- Umeå universitet,Kemiska institutionen
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Sizun, Christina (författare)
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Koch, Joachim (författare)
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Herget, Meike (författare)
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Abele, Rupert (författare)
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Bechinger, Burkhard (författare)
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Tampé, Robert (författare)
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(creator_code:org_t)
- 2006
- 2006
- Engelska.
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Ingår i: The Journal of Biological Chemistry. - 0021-9258. ; 281:41, s. 30365-72
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- To evade the host's immune response, herpes simplex virus employs the immediate early gene product ICP47 (IE12) to suppress antigen presentation to cytotoxic T-lymphocytes by inhibition of the ATP-binding cassette transporter associated with antigen processing (TAP). ICP47 is a membrane-associated protein adopting an alpha-helical conformation. Its active domain was mapped to residues 3-34 and shown to encode all functional properties of the full-length protein. The active domain of ICP47 was reconstituted into oriented phospholipid bilayers and studied by proton-decoupled 15N and 2H solid-state NMR spectroscopy. In phospholipid bilayers, the protein adopts a helix-loop-helix structure, where the average tilt angle of the helices relative to the membrane surface is approximately 15 degrees (+/- 7 degrees ). The alignment of both structured domains exhibits a mosaic spread of approximately 10 degrees . A flexible dynamic loop encompassing residues 17 and 18 separates the two helices. Refinement of the experimental data indicates that helix 1 inserts more deeply into the membrane. These novel insights into the structure of ICP47 represent an important step toward a molecular understanding of the immune evasion mechanism of herpes simplex virus and are instrumental for the design of new therapeutics.
Nyckelord
- Cell Membrane/metabolism
- Dimerization
- Humans
- Immediate-Early Proteins/*chemistry
- Lipid Bilayers/chemistry
- Magnetic Resonance Spectroscopy
- Major Histocompatibility Complex
- Models; Molecular
- Protein Conformation
- Protein Structure; Secondary
- Protons
- Simplexvirus/metabolism
- T-Lymphocytes; Cytotoxic/virology
- Temperature
- Viral Proteins/*chemistry
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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