Source:http://linkedlifedata.com/resource/pubmed/id/18538660
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2008-6-9
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pubmed:databankReference | |
pubmed:abstractText |
Key to the pathogenicity of several viruses is activation of the canonical nuclear factor-kappaB (NF-kappaB) transcriptional pathway. Subversion of this tightly regulated mechanism is achieved through the production of host mimetic viral proteins that deregulate the transcription process. One such protein is ks-vFLIP (produced by the Kaposi's sarcoma herpes virus [KSHV]), which associates with IKKgamma, an essential component of the IKK complex or signalosome. This interaction renders the canonical NF-kappaB pathway constitutively active and has been linked to Kaposi's sarcoma and other malignancies. In order to elucidate the molecular basis underpinning ks-vFLIP-induced activation of the IKK signalosome, we have determined the crystal structure of a complex involving a fragment of IKKgamma bound to ks-vFLIP at 3.2 A. In addition to identifying and subsequently probing the ks-vFLIP-IKKgamma interface, we have also investigated the effects of a mutation implicated in the genetic disorder anhydrotic ectodermal dysplasia with immunodeficiency (EDA-ID).
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/viral FLIP protein, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1097-4164
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
6
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
620-31
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18538660-Amino Acid Sequence,
pubmed-meshheading:18538660-Animals,
pubmed-meshheading:18538660-Crystallography, X-Ray,
pubmed-meshheading:18538660-Ectodermal Dysplasia,
pubmed-meshheading:18538660-Herpesvirus 8, Human,
pubmed-meshheading:18538660-Humans,
pubmed-meshheading:18538660-I-kappa B Kinase,
pubmed-meshheading:18538660-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:18538660-Molecular Sequence Data,
pubmed-meshheading:18538660-Mutagenesis, Site-Directed,
pubmed-meshheading:18538660-NF-kappa B,
pubmed-meshheading:18538660-Protein Binding,
pubmed-meshheading:18538660-Protein Conformation,
pubmed-meshheading:18538660-Sequence Alignment,
pubmed-meshheading:18538660-Signal Transduction,
pubmed-meshheading:18538660-Viral Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
Crystal structure of a vFlip-IKKgamma complex: insights into viral activation of the IKK signalosome.
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pubmed:affiliation |
Institute of Structural and Molecular Biology, School of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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