6SAI
NMR solution structure of Hml-2 C-terminal dimer domain
Summary for 6SAI
| Entry DOI | 10.2210/pdb6sai/pdb |
| Related | 6SA9 |
| NMR Information | BMRB: 34419 |
| Descriptor | Gag protein (1 entity in total) |
| Functional Keywords | human-endogenous-retroviruses, retroviridae, ortervirales., viral protein |
| Biological source | Human endogenous retrovirus K |
| Total number of polymer chains | 2 |
| Total formula weight | 20187.23 |
| Authors | Nicastro, G.,Taylor, I.A.,Ball, N.J.,Ramos, A. (deposition date: 2019-07-16, release date: 2020-01-15, Last modification date: 2024-05-15) |
| Primary citation | Acton, O.,Grant, T.,Nicastro, G.,Ball, N.J.,Goldstone, D.C.,Robertson, L.E.,Sader, K.,Nans, A.,Ramos, A.,Stoye, J.P.,Taylor, I.A.,Rosenthal, P.B. Structural basis for Fullerene geometry in a human endogenous retrovirus capsid. Nat Commun, 10:5822-5822, 2019 Cited by PubMed Abstract: The HML2 (HERV-K) group constitutes the most recently acquired family of human endogenous retroviruses, with many proviruses less than one million years old. Many maintain intact open reading frames and provirus expression together with HML2 particle formation are observed in early stage human embryo development and are associated with pluripotency as well as inflammatory disease, cancers and HIV-1 infection. Here, we reconstruct the core structural protein (CA) of an HML2 retrovirus, assemble particles in vitro and employ single particle cryogenic electron microscopy (cryo-EM) to determine structures of four classes of CA Fullerene shell assemblies. These icosahedral and capsular assemblies reveal at high-resolution the molecular interactions that allow CA to form both pentamers and hexamers and show how invariant pentamers and structurally plastic hexamers associate to form the unique polyhedral structures found in retroviral cores. PubMed: 31862888DOI: 10.1038/s41467-019-13786-y PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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