2KOD
A high-resolution NMR structure of the dimeric C-terminal domain of HIV-1 CA
Summary for 2KOD
| Entry DOI | 10.2210/pdb2kod/pdb |
| Descriptor | HIV-1 CA C-terminal domain (1 entity in total) |
| Functional Keywords | hiv-1 capsid, c-terminal domain, viral protein |
| Biological source | HIV-1 M:B_HXB2R (HIV-1) |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P04585 |
| Total number of polymer chains | 2 |
| Total formula weight | 19678.63 |
| Authors | Byeon, I.-J.L.,Jung, J.,Ahn, J.,concel, J.,Gronenborn, A.M. (deposition date: 2009-09-18, release date: 2009-11-24, Last modification date: 2024-05-01) |
| Primary citation | Byeon, I.J.,Meng, X.,Jung, J.,Zhao, G.,Yang, R.,Ahn, J.,Shi, J.,Concel, J.,Aiken, C.,Zhang, P.,Gronenborn, A.M. Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell(Cambridge,Mass.), 139:780-790, 2009 Cited by PubMed Abstract: Mature HIV-1 particles contain conical-shaped capsids that enclose the viral RNA genome and perform essential functions in the virus life cycle. Previous structural analysis of two- and three-dimensional arrays of the capsid protein (CA) hexamer revealed three interfaces. Here, we present a cryoEM study of a tubular assembly of CA and a high-resolution NMR structure of the CA C-terminal domain (CTD) dimer. In the solution dimer structure, the monomers exhibit different relative orientations compared to previous X-ray structures. The solution structure fits well into the EM density map, suggesting that the dimer interface is retained in the assembled CA. We also identified a CTD-CTD interface at the local three-fold axis in the cryoEM map and confirmed its functional importance by mutagenesis. In the tubular assembly, CA intermolecular interfaces vary slightly, accommodating the asymmetry present in tubes. This provides the necessary plasticity to allow for controlled virus capsid dis/assembly. PubMed: 19914170DOI: 10.1016/j.cell.2009.10.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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