9NZ5
MERSmut-CoV M protein dimer in complex with FAb B
Summary for 9NZ5
| Entry DOI | 10.2210/pdb9nz5/pdb |
| EMDB information | 49951 |
| Descriptor | Membrane protein, FAb B light chain, FAb B heavy chain (3 entities in total) |
| Functional Keywords | m protein, sars-cov-2, inhibitor bound complex, viral protein, membrane protein-immune system-inhibitor complex, membrane protein/immune system/inhibitor |
| Biological source | Middle East respiratory syndrome-related coronavirus More |
| Total number of polymer chains | 6 |
| Total formula weight | 155821.41 |
| Authors | Mann, M.K.,Abeywickrema, P. (deposition date: 2025-03-31, release date: 2025-10-29, Last modification date: 2025-12-10) |
| Primary citation | Mann, M.K.,Yin, Y.,Marsili, S.,Xie, J.,Doijen, J.,Miller, R.,Piassek, M.,van den Broeck, N.,Kariuki, C.K.,de Gruyter, H.L.M.,Leijs, A.A.,Snijder, E.J.,van Hemert, M.J.,Keustermans, K.,Van Gool, M.,Yu, X.,Loock, M.V.,Koul, A.,Sharma, S.,Van Damme, E.,Abeywickrema, P. Structural insights into MERS and SARS coronavirus membrane proteins. Commun Biol, 8:1651-1651, 2025 Cited by PubMed Abstract: The membrane (M) protein of coronaviruses is essential for maintaining structural integrity during membrane virion budding and viral pathogenesis. Given its high conservation in lineages within the betacoronavirus genus, such as sarbecoviruses, the M protein presents as an attractive therapeutic target; however, developing broad-spectrum antivirals targeting coronaviruses such as MERS-CoV is challenging due to lower sequence conservation and limited structural information available beyond that of the SARS-CoV-2 M protein. In this study, we report 3-3.2 Å resolution structures of MERS-CoV M protein, engineered with a SARS-CoV-2-like antibody interface, representing the first human merbecovirus M protein structure, and SARS-CoV M protein structures, with and without a previously identified SARS-CoV-2 M protein inhibitor, JNJ-9676. We highlight the structural differences between the MERS-CoV, SARS-CoV and SARS-CoV-2 M proteins, and present insights into the conservation of the JNJ-9676 binding pocket as well as key differences that could be targeted to accelerate the design of specific MERS-CoV and broad-spectrum antivirals targeting coronavirus M proteins. PubMed: 41286109DOI: 10.1038/s42003-025-09042-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.15 Å) |
Structure validation
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