EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Mechanisms of HSV-1 helicase-primase inhibition and replication fork complex assembly.
ジャーナル・号・ページ	Cell, Vol. 189, Issue 2, Page 478-494.e18, Year 2026
掲載日	2026年1月22日
著者	Zishuo Yu / Pradeep Sathyanarayana / Cong Liu / Joel M J Tan / Pan Yang / Biswajit Das / Side Hu / Xiaoyi Fan / Chenggong Ji / Sandra K Weller / Mrinal Shekhar / Donald M Coen / Philip J Kranzusch / Joseph J Loparo / Jonathan Abraham /
PubMed 要旨	Herpesviruses are widespread double-stranded DNA viruses that establish lifelong latency and cause various diseases. Although DNA-polymerase-targeting antivirals are effective, increasing drug ...Herpesviruses are widespread double-stranded DNA viruses that establish lifelong latency and cause various diseases. Although DNA-polymerase-targeting antivirals are effective, increasing drug resistance underscores the need for alternatives. Helicase-primase inhibitors (HPIs) are promising antivirals, but their mechanisms of action are poorly defined. Furthermore, how the helicase-primase (H/P) complex and DNA polymerase coordinate genome replication is not well understood for herpesviruses. Here, we report cryo-electron microscopy (cryo-EM) structures of the herpes simplex virus 1 H/P complex bound to HPIs, showing that these lock the H/P complex in an inactive state. Single-molecule assays reveal that HPIs cause H/P complexes to pause in unwinding activity on DNA. The structure of an HPI-bound replication fork complex, comprising the H/P complex (UL5, UL52, and UL8) and the polymerase holoenzyme (UL30 and UL42), reveals a previously uncharacterized interface bridging these complexes. These findings provide a structural framework for understanding herpesvirus replisome assembly and advancing inhibitor development.
リンク	Cell / PubMed:41468884 / PubMed Central
手法	EM (単粒子)
解像度	2.55 - 6.6 Å
構造データ	EMDB-72754: Local refinement of HSV UL5 in HSV replication fork complex 手法: EM (単粒子) / 解像度: 3.5 Å EMDB-72755: Local refinement of HSV UL30 in HSV replication fork complex 手法: EM (単粒子) / 解像度: 3.6 Å EMDB-72757: Low resolution map of HSV replication fork complex 手法: EM (単粒子) / 解像度: 6.6 Å EMDB-72758: Local refinement of interface of HSV UL5 and UL30 in the replication fork 手法: EM (単粒子) / 解像度: 3.7 Å 72764 9yc9 EMDB-72764, PDB-9yc9: HSV replication fork complex bound to pritelivir 手法: EM (単粒子) / 解像度: 3.8 Å EMDB-72780: Local refinement of HSV UL5 in IM-250 bound H/P complex 手法: EM (単粒子) / 解像度: 3.2 Å 72781 9ycp EMDB-72781, PDB-9ycp: HSV Helicase-primase complex bound to IM-250 手法: EM (単粒子) / 解像度: 2.9 Å EMDB-72784: Local refinment of HSV UL5 in pritelivir-bound H/P complex 手法: EM (単粒子) / 解像度: 3.35 Å EMDB-72785: Local refinement of HSV UL8 in pritelivir-bound H/P complex 手法: EM (単粒子) / 解像度: 3.3 Å 72786 9yct EMDB-72786, PDB-9yct: HSV helicase-primase complex bound to pritelivir 手法: EM (単粒子) / 解像度: 3.7 Å EMDB-72787: Local refinement of HSV UL5 in amenamevir-bound H/P complex 手法: EM (単粒子) / 解像度: 2.55 Å EMDB-72788: Local refinement of HSV UL8 in amenamevir-bound H/P complex 手法: EM (単粒子) / 解像度: 2.6 Å 72789 9ycv EMDB-72789, PDB-9ycv: HSV Helicase-primase complex bound to amenamevir 手法: EM (単粒子) / 解像度: 2.8 Å
化合物	ChemComp-ZN: Unknown entry PDB-1bxb: XYLOSE ISOMERASE FROM THERMUS THERMOPHILUS PDB 未公開エントリ PDB-1chb: Unknown entry PDB-1bxd: NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ
由来	human alphaherpesvirus 1 strain r-15 (ヘルペスウイルス)
キーワード	VIRAL PROTEIN / HSV / replisome / replication / helicase-primase complex / helicase-primase / pritelivir / HPI