4u4h

Crystal Structure of HSV-1 UL21 N-terminal Domain

spinqualitylabelsall models 4u4h, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4u4h is a 1 chain structure with sequence from Human alphaherpesvirus 1 strain 17. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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