7N1H
CryoEM structure of Venezuelan equine encephalitis virus VLP in complex with the LDLRAD3 receptor
This is a non-PDB format compatible entry.
Summary for 7N1H
| Entry DOI | 10.2210/pdb7n1h/pdb |
| EMDB information | 24116 24394 |
| Descriptor | Low-density lipoprotein receptor class A domain-containing protein 3, E1 envelope glycoprotein, E2 envelope glycoprotein, ... (6 entities in total) |
| Functional Keywords | veev, viral envelope, host receptor, low-density lipoprotein receptor type-a module, ldlrad3, encephalitic alphavirus, structural genomics, center for structural genomics of infectious diseases, csgid, virus like particle |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 16 |
| Total formula weight | 472228.03 |
| Authors | Basore, K.,Nelson, C.A.,Fremont, D.H.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2021-05-27, release date: 2021-10-13, Last modification date: 2024-11-20) |
| Primary citation | Basore, K.,Ma, H.,Kafai, N.M.,Mackin, S.,Kim, A.S.,Nelson, C.A.,Diamond, M.S.,Fremont, D.H. Structure of Venezuelan equine encephalitis virus in complex with the LDLRAD3 receptor. Nature, 598:672-676, 2021 Cited by PubMed Abstract: LDLRAD3 is a recently defined attachment and entry receptor for Venezuelan equine encephalitis virus (VEEV), a New World alphavirus that causes severe neurological disease in humans. Here we present near-atomic-resolution cryo-electron microscopy reconstructions of VEEV virus-like particles alone and in a complex with the ectodomains of LDLRAD3. Domain 1 of LDLRAD3 is a low-density lipoprotein receptor type-A module that binds to VEEV by wedging into a cleft created by two adjacent E2-E1 heterodimers in one trimeric spike, and engages domains A and B of E2 and the fusion loop in E1. Atomic modelling of this interface is supported by mutagenesis and anti-VEEV antibody binding competition assays. Notably, VEEV engages LDLRAD3 in a manner that is similar to the way that arthritogenic alphaviruses bind to the structurally unrelated MXRA8 receptor, but with a much smaller interface. These studies further elucidate the structural basis of alphavirus-receptor interactions, which could inform the development of therapies to mitigate infection and disease against multiple members of this family. PubMed: 34646020DOI: 10.1038/s41586-021-03963-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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