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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2009-11-5
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pubmed:databankReference |
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pubmed:abstractText |
The poxvirus 2L protein binds tumor necrosis factor-alpha (TNFalpha) to inhibit host antiviral and immune responses. The 2.8-A 2L-TNFalpha structure reveals three symmetrically arranged 2L molecules per TNFalpha trimer. 2L resembles class I major histocompatibility complex (MHC) molecules but lacks a peptide-binding groove and beta2-microglobulin light chain. Overlap between the 2L and host TNF receptor-binding sites on TNFalpha rationalizes 2L inhibition of TNFalpha-TNF receptor interactions and prevention of TNFalpha-induced immune responses.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-10367903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-12543935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-12676996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-14512626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-15012932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-15737590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-16089503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-16518473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-17195034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-17681535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-18632577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-19084540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-19232662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-8253759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-8263940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-8387891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-8552589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19838188-9546397
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1545-9985
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1189-91
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pubmed:dateRevised |
2010-9-28
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pubmed:meshHeading |
pubmed-meshheading:19838188-Binding Sites,
pubmed-meshheading:19838188-Histocompatibility Antigens Class I,
pubmed-meshheading:19838188-Humans,
pubmed-meshheading:19838188-Models, Molecular,
pubmed-meshheading:19838188-Poxviridae,
pubmed-meshheading:19838188-Protein Binding,
pubmed-meshheading:19838188-Protein Structure, Secondary,
pubmed-meshheading:19838188-Tumor Necrosis Factor-alpha,
pubmed-meshheading:19838188-Viral Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein.
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pubmed:affiliation |
Division of Biology 114-96, California Institute of Technology, Pasadena, California, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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