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	TMPRSS2-mediated coronavirus spike activation and inhibition.
Journal, issue, pages	Nat Struct Mol Biol, Year 2026
Publish date	Apr 28, 2026
Authors	Matthew McCallum / James Brett Case / Jack T Brown / Young-Jun Park / Jimin Lee / Emmajay Sutherland / Anupriya Aggarwal / Cecily Gibson / Florian A Lempp / Cameron Stewart / M Alejandra Tortorici / Shilpa Sanapala / Jun Siong Low / Daniel Asarnow / Dana Bohan / Exequiel Dellota / Benjamin Merz / Bhavna Chawla / Swagata Kar / Antonio Lanzavecchia / Federica Sallusto / Nicholas M Riley / Stuart Turville / Lisa Purcell / Michael S Diamond / David Veesler /
PubMed Abstract	The protease TMPRSS2 facilitates coronavirus infections, yet its mechanism of viral glycoprotein recognition remains unclear. Here we show that, following ACE2 engagement of the SARS-CoV-2 spike (S) ...The protease TMPRSS2 facilitates coronavirus infections, yet its mechanism of viral glycoprotein recognition remains unclear. Here we show that, following ACE2 engagement of the SARS-CoV-2 spike (S) inducing the early fusion intermediate conformation (E-FIC), TMPRSS2 cleaves the R815 S' site and promotes fusogenic conformational changes leading to viral entry. We unveil TMPRSS2 recognition of S', identify key residues modulating binding specificity and demonstrate that S' site-directed broadly neutralizing antibodies target E-FIC and inhibit viral entry by blocking TMPRSS2 access. We computationally designed stabilized E-FIC as a vaccine candidate, overcoming the transient nature of this state. We describe a TMPRSS2-directed monoclonal antibody inhibiting several coronaviruses, including SARS-CoV-2 variants and protecting mice against SARS-CoV-2 challenge. These results outline the mechanistic role of TMPRSS2 and S' site-directed antibodies in coronavirus entry.
External links	Nat Struct Mol Biol / PubMed:42050172
Methods	EM (single particle)
Resolution	2.7 - 3.8 Å
Structure data	70721 9opq EMDB-70721, PDB-9opq: TMPRSS2 (S441A) bound to the HCoV-NL63 S2'region genetically fused to the HCoV-HKU1 RBD Method: EM (single particle) / Resolution: 3.3 Å 70722 9opr EMDB-70722, PDB-9opr: TMPRSS2 S441A in complex with the H1H7 Fab and anti-kappa light chain nanobody Method: EM (single particle) / Resolution: 3.2 Å 73656 9yyu EMDB-73656, PDB-9yyu: SARS-CoV-2 spike trimer in the early fusion intermediate conformation bound to the VN01H1 Fab (Fab local refinement) Method: EM (single particle) / Resolution: 3.3 Å 73657 9yyv EMDB-73657, PDB-9yyv: SARS-CoV-2 spike trimer in the early fusion intermediate conformation bound to the VN01H1 Fab (S2 local refinement) Method: EM (single particle) / Resolution: 3.3 Å 73786 9z3j EMDB-73786, PDB-9z3j: HCoV-NL63 S2' peptide bound to TMPRSS2 S441A (complexed with the H1H7 Fab and an anti-kappa-nanobody) Method: EM (single particle) / Resolution: 2.8 Å 73787 9z3k EMDB-73787, PDB-9z3k: SARS-CoV-2 S2 trimer stabilized in the early fusion intermediate conformation by circular permutation and clamping by gp41 (E-FICs-v1) Method: EM (single particle) / Resolution: 3.3 Å EMDB-75233: SARS-CoV-2 spike trimer in the early fusion intermediate conformation bound to the VN01H1 Fab (global refinement) Method: EM (single particle) / Resolution: 3.8 Å 75694 11hk EMDB-75694, PDB-11hk: SARS-CoV-2 spike S2 trimer stabilized in the early fusion intermediate conformation (E-FICs-v3) bound to the VN01H1 Fab (Fab local refinement) Method: EM (single particle) / Resolution: 2.7 Å 75695 11hl EMDB-75695, PDB-11hl: SARS-CoV-2 spike S2 trimer stabilized in the early fusion intermediate conformation (E-FICs-v3) bound to the VN01H1 Fab (S2 local refinement) Method: EM (single particle) / Resolution: 2.8 Å 75697 11hn EMDB-75697, PDB-11hn: SARS-CoV-2 spike S2 trimer stabilized in the early fusion intermediate conformation (E-FICs-v3) bound to C77G12 (S2 local refinement) Method: EM (single particle) / Resolution: 2.7 Å 75705 11hw EMDB-75705, PDB-11hw: SARS-CoV-2 spike S2 trimer stabilized in the early fusion intermediate conformation (E-FICs-v3) bound to C77G12 (Fab local refinement) Method: EM (single particle) / Resolution: 2.8 Å EMDB-75721: SARS-CoV-2 spike S2 trimer stabilized in the early fusion intermediate conformation (E-FICs-v3) bound to the VN01H1 Fab Method: EM (single particle) / Resolution: 2.9 Å EMDB-75722: SARS-CoV-2 spike S2 trimer stabilized in the early fusion intermediate conformation (E-FICs-v3) bound to C77G12 (global refinement) Method: EM (single particle) / Resolution: 2.9 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-HOH: WATER
Source	homo sapiens (human) human coronavirus hku1 lama glama (llama) severe acute respiratory syndrome coronavirus 2 human coronavirus nl63 SARS-CoV-2 pseudovirus saccharomyces cerevisiae s288c (yeast)
Keywords	VIRAL PROTEIN / S2prime / coronavirus / SARS-CoV-2 / spike / fusion / entry / antiviral / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / VIRAL PROTEIN-HYDROLASE complex / VN01H1 / C77G12 / VIRAL PROTEIN complex / VIRAL PROTEIN/HYDROLASE / TMPRSS2 / NL63 / HKU1 / RBD / cleavage / protease / HYDROLASE/IMMUNE SYSTEM / H1H7 / nanobody / antibody / HYDROLASE-IMMUNE SYSTEM complex / VIRAL PROTEIN/IMMUNE SYSTEM / Virus / coronaviruses / E-FIC / ACE2 / Glycoprotein / Receptor / VIRAL PROTEIN-IMMUNE SYSTEM complex