A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formation.

@article{Nellissery2007APL,
  title={A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formation.},
  author={Jacob K Nellissery and Renata Szczepaniak and Carmela Lamberti and Sandra K Weller},
  journal={Journal of virology},
  year={2007},
  volume={81 17},
  pages={
          8868-77
        }
}
The herpes simplex virus type 1 UL6 protein forms a 12-subunit ring structure at a unique capsid vertex which functions as a conduit for encapsidation of the viral genome. To characterize UL6 protein domains that are involved in intersubunit interactions and interactions with other capsid proteins, we engineered a set of deletion mutants spanning the entire gene. Three deletion constructs, D-5 (Delta 198-295), D-6 (Delta 322-416), and D-LZ (Delta 409-473, in which a putative leucine zipper was… CONTINUE READING
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