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-Structure paper
タイトル | Structure of the measles virus ternary polymerase complex. |
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ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 3819, Year 2025 |
掲載日 | 2025年4月23日 |
![]() | Dong Wang / Ge Yang / Bin Liu / ![]() |
PubMed 要旨 | Measles virus (MeV) is a highly contagious pathogen that causes significant morbidity worldwide. Its polymerase machinery, composed of the large protein (L) and phosphoprotein (P), is crucial for ...Measles virus (MeV) is a highly contagious pathogen that causes significant morbidity worldwide. Its polymerase machinery, composed of the large protein (L) and phosphoprotein (P), is crucial for viral replication and transcription, making it a promising target for antiviral drug development. Here we present cryo-electron microscopy structures of two distinct MeV polymerase complexes: L-P and L-P-C. The L-P complex characterizes the N-terminal domain, RNA-dependent RNA polymerase (RdRp), and GDP poly-ribonucleotidyltransferase of the L protein, along with the tetrameric P of varying lengths. The L-P-C complex reveals that C protein dimer binds at the cleft between RdRp and the flexible domains of the L protein: the connecting domain, methyltransferase domain, and C-terminal domain. This interaction results in the visualization of these domains and creates an extended RNA channel, remodeling the putative nascent replicated RNA exit and potentially regulating RNA synthesis processivity. Our findings reveal the architecture and molecular details of MeV polymerase complexes, providing new insights into their mechanisms and suggesting potential intervention targets for antiviral therapy. |
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手法 | EM (単粒子) |
解像度 | 3.12 - 3.3 Å |
構造データ | EMDB-47176, PDB-9dus: EMDB-47177, PDB-9dut: |
由来 |
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![]() | TRANSFERASE / VIRAL PROTEIN / Measles virus / L protein / phosphoprotein / RNA-dependent RNA polymerase / PRNTase / GDP polyribonucleotidyl transferase / RNA capping / MTase / viral replication / C protein |