2C9L
Structure of the Epstein-Barr virus ZEBRA protein
2C9L の概要
| エントリーDOI | 10.2210/pdb2c9l/pdb |
| 関連するPDBエントリー | 1ZSD 2AXF 2AXG 2C9N |
| 分子名称 | 5'-D(*AP*AP*GP*CP*AP*CP*TP*GP*AP*CP *TP*CP*AP*TP*GP*AP*AP*GP*T)-3', 5'-D(*AP*CP*TP*TP*CP*AP*CP*TP*GP*AP *GP*TP*CP*AP*GP*TP*GP*CP*T)-3', BZLF1 TRANS-ACTIVATOR PROTEIN, ... (4 entities in total) |
| 機能のキーワード | viral protein, epstein-barr virus, ebv, zebra, bzlf1, zta, z, lytic cycle activation, bzip protein, viral protein dna-binding, nuclear protein, transcription regulation |
| 由来する生物種 | HUMAN HERPESVIRUS 4 詳細 |
| 細胞内の位置 | Host nucleus: 2C9L |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 26171.87 |
| 構造登録者 | Petosa, C.,Morand, P.,Baudin, F.,Moulin, M.,Artero, J.B.,Muller, C.W. (登録日: 2005-12-13, 公開日: 2006-02-21, 最終更新日: 2023-12-13) |
| 主引用文献 | Petosa, C.,Morand, P.,Baudin, F.,Moulin, M.,Artero, J.B.,Muller, C.W. Structural Basis of Lytic Cycle Activation by the Epstein-Barr Virus Zebra Protein Mol.Cell, 21:565-, 2006 Cited by PubMed Abstract: Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to several human malignancies. EBV has a biphasic infection cycle consisting of a latent and a lytic, replicative phase. The switch from latent to lytic infection is triggered by the EBV immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). We present the crystal structure of ZEBRA's DNA binding domain bound to an EBV lytic gene promoter element. ZEBRA exhibits a variant of the basic-region leucine zipper (bZIP) fold in which a C-terminal moiety stabilizes the coiled coil involved in dimer formation. The structure provides insights into ZEBRA's broad target site specificity, preferential activation of specific EBV promoters in their methylated state, ability to dimerize despite lacking a leucine zipper motif, and failure to heterodimerize with cellular bZIP proteins. The structure will allow for the design of new therapeutic agents that block activation of the EBV lytic cycle. PubMed: 16483937DOI: 10.1016/J.MOLCEL.2006.01.006 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.25 Å) |
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