6lnl

ASFV core shell protein p15

spinqualitylabelsall models 6lnl, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lnl is a 3 chain structure with sequence from African swine fever virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9286Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PP62_ASFB7 Essential for the correct assembly and maturation of the core of the virion. Component of the core shell (PubMed:30185597). Binds to phosphatidylserine, which may enable the core shell binding with the inner membrane (PubMed:32519301). Component of the core shell (PubMed:30185597). Binds to phosphatidylserine and DNA, which may link the core shell to the inner membrane and to the viral nucleoid (PubMed:32451720). Component of the core shell. Publication Abstract from PubMed African swine fever (ASF) is an acute, hemorrhagic, and highly contagious disease caused by African swine fever virus (ASFV). The mortality rate of acute infection up to 100% have posed an unprecedented challenge of the swine industry. Currently no commercial antiviral drug is available for the control and treatment of ASFV. The structural resolution of ASFV virions reveals the details of ASFV morphogenesis, providing a new perspective for the research and promotion of the development of ASFV vaccines. Although the architecture of ASFV have been solved via cryo-EM, the structural details of four of the five viral layers remain unclear (except the outer capsid). In this study, we resolved the crystal structure of the ASFV core shell protein p15. The secondary structural elements of a protomer include four alpha-helix structures and six antiparallel beta-strands. Further analysis revealed that ASFV p15 forms disulfide-linked trimers between the Cys9 from one protomer and Cys30 from other protomer. Additionally, the nucleic acid-binding property was characterized by electrophoretic mobility shift assay. Two critical amino acid Lys10 and Lys39 have been identified which is essential to the nucleic acid-binding affinity of ASFV p15. Together, these findings may provide new insight into antiviral drug development. The structural basis of African swine fever virus core shell protein p15 binding to DNA.,Guo F, Shi Y, Yang M, Guo Y, Shen Z, Li M, Chen Y, Liang R, Yang Y, Chen H, Peng G FASEB J. 2021 Mar;35(3):e21350. doi: 10.1096/fj.202002145R. PMID:33629764 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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