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-Structure paper
タイトル | Structural basis for nuclear import of hepatitis B virus (HBV) nucleocapsid core. |
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ジャーナル・号・ページ | Sci Adv, Vol. 10, Issue 2, Page eadi7606, Year 2024 |
掲載日 | 2024年1月12日 |
![]() | Ruoyu Yang / Ying-Hui Ko / Fenglin Li / Ravi K Lokareddy / Chun-Feng David Hou / Christine Kim / Shelby Klein / Santiago Antolínez / Juan F Marín / Carolina Pérez-Segura / Martin F Jarrold / Adam Zlotnick / Jodi A Hadden-Perilla / Gino Cingolani / ![]() |
PubMed 要旨 | Nuclear import of the hepatitis B virus (HBV) nucleocapsid is essential for replication that occurs in the nucleus. The ~360-angstrom HBV capsid translocates to the nuclear pore complex (NPC) as an ...Nuclear import of the hepatitis B virus (HBV) nucleocapsid is essential for replication that occurs in the nucleus. The ~360-angstrom HBV capsid translocates to the nuclear pore complex (NPC) as an intact particle, hijacking human importins in a reaction stimulated by host kinases. This paper describes the mechanisms of HBV capsid recognition by importins. We found that importin α1 binds a nuclear localization signal (NLS) at the far end of the HBV coat protein Cp183 carboxyl-terminal domain (CTD). This NLS is exposed to the capsid surface through a pore at the icosahedral quasi-sixfold vertex. Phosphorylation at serine-155, serine-162, and serine-170 promotes CTD compaction but does not affect the affinity for importin α1. The binding of 30 importin α1/β1 augments HBV capsid diameter to ~620 angstroms, close to the maximum size trafficable through the NPC. We propose that phosphorylation favors CTD externalization and prompts its compaction at the capsid surface, exposing the NLS to importins. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 1.99 - 3.8 Å |
構造データ | EMDB-29756, PDB-8g5v: EMDB-29785, PDB-8g6v: EMDB-29858, PDB-8g8y: ![]() PDB-7umi: |
化合物 | ![]() ChemComp-HOH: |
由来 |
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![]() | PROTEIN TRANSPORT / nuclear import / viral replication / peptide binding / nuclear localization signal binding / NUCLEAR PROTEIN / VIRUS LIKE PARTICLE / Virus capsid / complex formed by viral capsid and importin / Capsid formed by Cp183 when bound to importin alpha1 |