Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Strategic variations in sarbecovirus and merbecovirus Nsp1 linker regions for translation inhibition.
Journal, issue, pages	Nucleic Acids Res, Vol. 54, Issue 2, Year 2026
Publish date	Jan 14, 2026
Authors	Ruixi Yan / Mingbo Wu / Xiangyu Ge / Qianqian Jin / Moyu Wang / Haolong Zhou / Yan Li / Yue Wang / Shuai Yuan /
PubMed Abstract	Nonstructural protein 1 (Nsp1) is a key virulence factor of coronaviruses, and its stable binding to the 40S ribosomal mRNA entry channel facilitates multiple functions, including suppression of host ...Nonstructural protein 1 (Nsp1) is a key virulence factor of coronaviruses, and its stable binding to the 40S ribosomal mRNA entry channel facilitates multiple functions, including suppression of host immune responses and degradation of host mRNA. To understand the structural basis of the conserved protein across viral lineages, we determined the cryo-EM structures of Nsp1-40S complexes of four coronaviruses from wild animals. Our results show that all Nsp1 proteins engage the mRNA entry channel via their C-terminal domain (CTD), but do not fully restrict the rotational mobility of the 40S head, which retains ∼5° of movement and repositions the Nsp1 linker region. Comparative analysis revealed distinct patterns in the linker regions connecting the N- and CTDs. Sarbecovirus Nsp1 contains a longer linker, whereas the merbecovirus Nsp1 adopts a shorter linker that navigates structural constraints more readily. Functionally, we find that linker length correlates with translation inhibition efficiency, suggesting a structural tuning mechanism. Additionally, variations in linker and helix 1 of the CTD among different lineages may serve as molecular markers for viral classification. Together, our results provide a comparative structural framework for understanding how coronavirus Nsp1 proteins modulate host translation and reflect evolutionary adaptations in ribosome engagement.
External links	Nucleic Acids Res / PubMed:41538319 / PubMed Central
Methods	EM (single particle)
Resolution	2.65 - 2.89 Å
Structure data	62444 9kmt EMDB-62444, PDB-9kmt: Bat SARSr-CoV RaTG15 Nsp1 bound to the Human 40S Ribosomal subunit-State1 Method: EM (single particle) / Resolution: 2.81 Å 62445 9kmu EMDB-62445, PDB-9kmu: Bat SARSr-CoV RaTG15 Nsp1 bound to the Human 40S Ribosomal subunit-State2 Method: EM (single particle) / Resolution: 2.87 Å 62446 9kmv EMDB-62446, PDB-9kmv: SARSr-MpCoV-GX Nsp1 bound to the Human 40S Ribosomal subunit-State1 Method: EM (single particle) / Resolution: 2.65 Å 62447 9kmw EMDB-62447, PDB-9kmw: SARSr-MpCoV-GX Nsp1 bound to the Human 40S Ribosomal subunit-State2 Method: EM (single particle) / Resolution: 2.73 Å 62448 9kmx EMDB-62448, PDB-9kmx: Bat MERSr-CoV NeoCoV Nsp1 bound to the Human 40S Ribosomal subunit-State1 Method: EM (single particle) / Resolution: 2.89 Å 62449 9kmy EMDB-62449, PDB-9kmy: Bat MERSr-CoV NeoCoV Nsp1 bound to the Human 40S Ribosomal subunit-State2 Method: EM (single particle) / Resolution: 2.7 Å 62450 9kmz EMDB-62450, PDB-9kmz: Bat MERSr-CoV NL140422 Nsp1 bound to the Human 40S Ribosomal subunit-State1 Method: EM (single particle) / Resolution: 2.78 Å 62451 9kn0 EMDB-62451, PDB-9kn0: Bat MERSr-CoV NL140422 Nsp1 bound to the Human 40S Ribosomal subunit-State2 Method: EM (single particle) / Resolution: 2.65 Å
Source	homo sapiens (human) sars bat coronavirus middle east respiratory syndrome-related coronavirus
Keywords	RIBOSOME / 40S / Nsp1 / betacoronaviruses / cryo-EM