Structural highlights
Function
[TEG4_HHV11] May participate in DNA packaging/capsid maturation events. Promotes efficient incorporation of tegument proteins UL46, UL49, and US3 into virions. May also play a role in capsid transport to the trans-Golgi network (TGN) (By similarity).
Publication Abstract from PubMed
UL21 is a conserved protein in the tegument in 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 Type 1 to 2.0-A resolution, which revealed a novel sail-like protein fold. Evolutionarily conserved surface patches highlight residues of potential importance for future targeting by mutagenesis.
The unusual fold of HSV-1 UL21, a multifunctional tegument protein.,Metrick CM, Chadha P, Heldwein EE J Virol. 2014 Dec 24. pii: JVI.03516-14. PMID:25540382[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Metrick CM, Chadha P, Heldwein EE. The unusual fold of HSV-1 UL21, a multifunctional tegument protein. J Virol. 2014 Dec 24. pii: JVI.03516-14. PMID:25540382 doi:http://dx.doi.org/10.1128/JVI.03516-14
