Bagneris, Claire and Ageichik, A.V. and Cronin, Nora and Wallace, Bonnie A. and Collins, M. and Boshoff, C. and Waksman, Gabriel and Barrett, Tracey E. (2008) Crystal structure of a vFlip-IKKγ Complex: insights into viral activation of the IKK Signalosome. Molecular Cell 30 (5), pp. 620-631. ISSN 1097-2765.
Abstract
Key to the pathogenicity of several viruses is activation of the canonical nuclear factor-κB (NF-κB) 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 IKKγ, an essential component of the IKK complex or signalosome. This interaction renders the canonical NF-κB 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 IKKγ bound to ks-vFLIP at 3.2 Å. In addition to identifying and subsequently probing the ks-vFLIP-IKKγ interface, we have also investigated the effects of a mutation implicated in the genetic disorder anhydrotic ectodermal dysplasia with immunodeficiency (EDA-ID).
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | SIGNALING, MOLIMMUNO |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Research Centres and Institutes: | Bioinformatics, Bloomsbury Centre for (Closed), Structural Molecular Biology, Institute of (ISMB) |
| Depositing User: | Administrator |
| Date Deposited: | 20 May 2013 11:29 |
| Last Modified: | 02 Aug 2023 17:04 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/6900 |
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