6NK3
Crystal structure of murine Mxra8 ectodomain
Summary for 6NK3
| Entry DOI | 10.2210/pdb6nk3/pdb |
| Related | 6NK6 6NK7 |
| Descriptor | Matrix remodeling-associated protein 8 (2 entities in total) |
| Functional Keywords | chikungunya, virus receptor, immunoglobulin-like, cell invasion, structural genomics, center for structural genomics of infectious diseases, csgid |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 62333.55 |
| Authors | Fremont, D.H.,Kim, A.S.,Nelson, C.A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2019-01-04, release date: 2019-05-22, Last modification date: 2024-10-23) |
| Primary citation | Basore, K.,Kim, A.S.,Nelson, C.A.,Zhang, R.,Smith, B.K.,Uranga, C.,Vang, L.,Cheng, M.,Gross, M.L.,Smith, J.,Diamond, M.S.,Fremont, D.H. Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor. Cell, 177:1725-, 2019 Cited by PubMed Abstract: Mxra8 is a receptor for multiple arthritogenic alphaviruses that cause debilitating acute and chronic musculoskeletal disease in humans. Herein, we present a 2.2 Å resolution X-ray crystal structure of Mxra8 and 4 to 5 Å resolution cryo-electron microscopy reconstructions of Mxra8 bound to chikungunya (CHIKV) virus-like particles and infectious virus. The Mxra8 ectodomain contains two strand-swapped Ig-like domains oriented in a unique disulfide-linked head-to-head arrangement. Mxra8 binds by wedging into a cleft created by two adjacent CHIKV E2-E1 heterodimers in one trimeric spike and engaging a neighboring spike. Two binding modes are observed with the fully mature VLP, with one Mxra8 binding with unique contacts. Only the high-affinity binding mode was observed in the complex with infectious CHIKV, as viral maturation and E3 occupancy appear to influence receptor binding-site usage. Our studies provide insight into how Mxra8 binds CHIKV and creates a path for developing alphavirus entry inhibitors. PubMed: 31080061DOI: 10.1016/j.cell.2019.04.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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