The Unusual Fold of Herpes Simplex Virus 1 UL21, a Multifunctional Tegument Protein

被引：17
|
作者：
Metrick, Claire M. [1 ,2 ]
Chadha, Pooja [3 ]
Heldwein, Ekaterina E. [1 ,2 ]
机构：
[1] Tufts Univ, Sch Med, Dept Mol Biol & Microbiol, Boston, MA 02111 USA
[2] Tufts Univ, Sch Med, Sackler Sch Grad Biomed Sci, Grad Program Biochem, Boston, MA 02111 USA
[3] Penn State Univ, Coll Med, Dept Microbiol & Immunol, Hershey, PA USA
来源：
JOURNAL OF VIROLOGY | 2015年 / 89卷 / 05期
关键词：
PSEUDORABIES VIRUS; BINDING; STRAIN; NEUROINVASION; PREDICTION; EFFECTOR; BARTHA; SPREAD; SERVER; CELLS;
D O I：
10.1128/JVI.03516-14
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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-angstrom resolution, which revealed a novel sail-like protein fold. Evolutionarily conserved surface patches highlight residues of potential importance for future targeting by mutagenesis.
引用
收藏
页码：2979 / 2984
页数：6
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