4U4H
Crystal Structure of HSV-1 UL21 N-terminal Domain
4U4H の概要
エントリーDOI | 10.2210/pdb4u4h/pdb |
分子名称 | Tegument protein UL21 (2 entities in total) |
機能のキーワード | viral protein |
由来する生物種 | Human herpesvirus 1 (HHV-1) |
細胞内の位置 | Virion tegument: P10205 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 23180.26 |
構造登録者 | |
主引用文献 | Metrick, C.M.,Chadha, P.,Heldwein, E.E. The Unusual Fold of Herpes Simplex Virus 1 UL21, a Multifunctional Tegument Protein. J.Virol., 89:2979-2984, 2015 Cited by PubMed Abstract: UL21 is a conserved protein in the tegument of alphaherpesviruses and has multiple important albeit poorly understood functions in viral replication and pathogenesis. To provide a roadmap for exploration of the multiple roles of UL21, we determined the crystal structure of its conserved N-terminal domain from herpes simplex virus 1 to 2.0-Å resolution, which revealed a novel sail-like protein fold. Evolutionarily conserved surface patches highlight residues of potential importance for future targeting by mutagenesis. PubMed: 25540382DOI: 10.1128/JVI.03516-14 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.05 Å) |
構造検証レポート
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