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-Structure paper
| タイトル | Activation of cytomegalovirus-encoded G protein-coupled receptor UL33 by an innate N-terminal peptide. |
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| ジャーナル・号・ページ | Commun Biol, Year 2026 |
| 掲載日 | 2026年2月12日 |
著者 | Anna K Drzazga / Shota Suzuki / Caroline Wouters / Felix Faas / Kouki Nishikawa / Akiko Kamegawa / Yoshinori Fujiyoshi / Mette M Rosenkilde / Naotaka Tsutsumi / ![]() |
| PubMed 要旨 | Human cytomegalovirus (HCMV) encodes the orphan G protein-coupled receptor (GPCR) UL33, which exhibits constitutive activity that disrupts host G protein signalling, facilitating efficient viral ...Human cytomegalovirus (HCMV) encodes the orphan G protein-coupled receptor (GPCR) UL33, which exhibits constitutive activity that disrupts host G protein signalling, facilitating efficient viral replication and pathogenesis. The cryo-electron microscopy (cryo-EM) structure of UL33 bound to the G subtype of G protein reveals the N-terminal peptide as a tethered ligand reminiscent of the protease-activated receptors and adhesion GPCRs. This self-agonism induces a non-canonical active state that facilitates promiscuous G protein coupling, a plausible viral strategy for fine-tuning host signalling. Structure-guided mutagenesis disrupting key interactions between the N-terminus and its binding pocket abolishes G protein-mediated signalling, confirming the role of the N-terminus as a self-agonist. Our findings elucidate the structural basis for this activation mechanism and highlight the strategies employed by HCMV to hijack host G protein signalling. |
リンク | Commun Biol / PubMed:41680497 |
| 手法 | EM (単粒子) |
| 解像度 | 3.3 Å |
| 構造データ | EMDB-65918, PDB-9wey: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / HCMV / viral protein / viral-host interaction / GPCR |
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万見文献について



著者

リンク

homo sapiens (ヒト)

human betaherpesvirus 5 (ヘルペスウイルス)
キーワード