3CL3
Crystal Structure of a vFLIP-IKKgamma complex: Insights into viral activation of the IKK signalosome
3CL3 の概要
| エントリーDOI | 10.2210/pdb3cl3/pdb |
| 分子名称 | ORF K13, NF-kappa-B essential modulator (2 entities in total) |
| 機能のキーワード | death effector domain, coiled-coil, coiled coil, cytoplasm, disease mutation, ectodermal dysplasia, host-virus interaction, nucleus, transcription, transcription regulation, viral protein-signaling protein complex, viral protein/signaling protein |
| 由来する生物種 | Human gammaherpesvirus 8 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 70846.87 |
| 構造登録者 | Bagneris, C.,Ageichik, A.V.,Cronin, N.,Boshoff, C.,Waksman, G.,Barrett, T. (登録日: 2008-03-18, 公開日: 2008-06-17, 最終更新日: 2024-02-21) |
| 主引用文献 | Bagneris, C.,Ageichik, A.V.,Cronin, N.,Wallace, B.,Collins, M.,Boshoff, C.,Waksman, G.,Barrett, T. Crystal structure of a vFlip-IKKgamma complex: insights into viral activation of the IKK signalosome. Mol.Cell, 30:620-631, 2008 Cited by PubMed Abstract: 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). PubMed: 18538660DOI: 10.1016/j.molcel.2008.04.029 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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