title: The unusual fold of herpes simplex virus 1 UL21, a multifunctional tegument protein.
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.
authors.affiliation: Department of Molecular Biology and Microbiology and Graduate Program in Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, Massachusetts, USA.
authors.forename: Claire M
authors.initials: CM
authors.lastname: Metrick
authors.affiliation: Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania, USA.
authors.forename: Pooja
authors.initials: P
authors.lastname: Chadha
authors.affiliation: Department of Molecular Biology and Microbiology and Graduate Program in Biochemistry, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, Massachusetts, USA katya.heldwein@tufts.edu.
authors.forename: Ekaterina E
authors.initials: EE
authors.lastname: Heldwein
mesh_terms: D018360:Crystallography, X-Ray; D018259:Herpesvirus 1, Human / Q000737:chemistry*; D006801:Humans; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D014764:Viral Proteins; C086728:UL21 protein, herpes simplex virus 1