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7YEQ

Structural insight into African Swine Fever Virus CP312R protein reveals it as a single-stranded DNA binding protein

Summary for 7YEQ
Entry DOI10.2210/pdb7yeq/pdb
DescriptorCP312R (2 entities in total)
Functional Keywordsafrican swine fever virus, cp312r, single-stranded dna binding protein, ob-fold, virus
Biological sourceAfrican swine fever virus (ASFV)
Total number of polymer chains1
Total formula weight34532.69
Authors
Chen, L.F.,Wu, Y.K. (deposition date: 2022-07-06, release date: 2023-07-26, Last modification date: 2026-03-04)
Primary citationChen, L.,Chen, L.,Chen, H.,Zhang, H.,Dong, P.,Sun, L.,Huang, X.,Lin, P.,Wu, L.,Jing, D.,Qian, Y.,Wu, Y.
Structural insights into the CP312R protein of the African swine fever virus.
Biochem.Biophys.Res.Commun., 624:68-74, 2022
Cited by
PubMed Abstract: African swine fever (ASF) is a lethal hemorrhagic disease that affects domestic pigs and wild boars. There is no medication available for ASF to date. The ability to mount antigen-specific responses to viral vectored CP312R makes it a crucial potential target for designing vaccines or drugs. This study determined the crystal structure of ASFV CP312R at 2.32 Å and found it to be a monomer with a single-stranded DNA binding core domain with a clear five-strands β-barrel OB-fold architecture. Electrophoretic mobility shift assay and size-exclusion chromatography characterization assay further confirmed the single-stranded DNA (ssDNA)-binding property of ASFV CP312R. This study revealed the structure and preliminary ssDNA interaction mechanisms of ASFV CP312R, providing new clues for developing new antiviral strategies.
PubMed: 35933928
DOI: 10.1016/j.bbrc.2022.07.091
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.32 Å)
Structure validation

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