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8BER

Hepatitis B virus core antigen (HBc) with the insertion of four external domains of the influenza A M2 protein (HBc/4M2e) with T=3 topology

8BER の概要
エントリーDOI10.2210/pdb8ber/pdb
EMDBエントリー16009
分子名称Core protein,Matrix protein 2,External core antigen (1 entity in total)
機能のキーワードhbc, m2e, vlp, virus like particle
由来する生物種Hepatitis B virus
詳細
タンパク質・核酸の鎖数3
化学式量合計92878.99
構造登録者
主引用文献Egorov, 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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4 Å)
構造検証レポート
Validation report summary of 8ber
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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