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PDBsum entry 2miz
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Viral protein
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PDB id
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2miz
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DOI no:
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Structure
22:1263-1273
(2014)
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PubMed id:
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The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family.
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N.G.Sgourakis,
K.Natarajan,
J.Ying,
B.Vogeli,
L.F.Boyd,
D.H.Margulies,
A.Bax.
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ABSTRACT
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Immunoevasins are key proteins used by viruses to subvert host immune responses.
Determining their high-resolution structures is key to understanding virus-host
interactions toward the design of vaccines and other antiviral therapies. Mouse
cytomegalovirus encodes a unique set of immunoevasins, the m02-m06 family, that
modulates major histocompatibility complex class I (MHC-I) antigen presentation
to CD8+ T cells and natural killer cells. Notwithstanding the large number of
genetic and functional studies, the structural biology of immunoevasins remains
incompletely understood, largely because of crystallization bottlenecks. Here we
implement a technology using sparse nuclear magnetic resonance data and
integrative Rosetta modeling to determine the structure of the m04/gp34
immunoevasin extracellular domain. The structure reveals a β fold that is
representative of the m02-m06 family of viral proteins, several of which are
known to bind MHC-I molecules and interfere with antigen presentation,
suggesting its role as a diversified immune regulation module.
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');
}
}
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