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8BDZ

Hepatitis B virus core antigen (HBc) with the insertion of four external domains of the influenza A M2 protein (HBc/4M2e) with T=4 topology

Summary for 8BDZ
Entry DOI10.2210/pdb8bdz/pdb
EMDB information15995
DescriptorCore protein,Matrix protein 2,External core antigen (1 entity in total)
Functional Keywordshbc, m2e, vlp, virus like particle
Biological sourceHepatitis B virus adw/991
More
Total number of polymer chains3
Total formula weight92581.60
Authors
Primary citationEgorov, V.V.,Shvetsov, A.V.,Pichkur, E.B.,Shaldzhyan, A.A.,Zabrodskaya, Y.A.,Vinogradova, D.S.,Nekrasov, P.A.,Gorshkov, A.N.,Garmay, Y.P.,Kovaleva, A.A.,Stepanova, L.A.,Tsybalova, L.M.,Shtam, T.A.,Myasnikov, A.G.,Konevega, A.L.
Inside and outside of virus-like particles HBc and HBc/4M2e: A comprehensive study of the structure.
Biophys.Chem., 293:106943-106943, 2022
Cited by
PubMed Abstract: Hepatitis B virus core antigen (HBc) with the insertion of four external domains of the influenza A M2 protein (HBc/4M2e) form virus-like particles whose structure was studied using a combination of molecular modeling and cryo-electron microscopy (cryo-EM). It was also shown that self-assembling of the particles occurs inside bacterial cells, but despite the big inner volume of the core shell particle, purified HBc/4M2e contain an insignificant amount of bacterial proteins. It was shown that a fragment of the M2e corresponding to 4M2e insertion is prone to formation of amyloid-like fibrils. However, as the part of the immunodominant loop, M2e insertion does not show a tendency to intermolecular interaction. A full-atomic HBc-4M2e model with the resolution of about 3 Å (3.13 Å for particles of Т = 4 symmetry, 3.7 Å for particles of Т = 3 symmetry) was obtained by molecular modeling methods based on cryo-EM data.
PubMed: 36495688
DOI: 10.1016/j.bpc.2022.106943
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.13 Å)
Structure validation

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数据于2024-11-06公开中

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