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From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TEG4_HHV11 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). | [[http://www.uniprot.org/uniprot/TEG4_HHV11 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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:25540382</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:01, 14 January 2015
Crystal Structure of HSV-1 UL21 N-terminal Domain
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