6OMT
HIV-1 capsid hexamer R18D mutant
Summary for 6OMT
| Entry DOI | 10.2210/pdb6omt/pdb |
| Descriptor | Capsid protein (2 entities in total) |
| Functional Keywords | hiv-1, capsid, ca, viral protein |
| Biological source | Human immunodeficiency virus 1 (HIV-1) |
| Total number of polymer chains | 1 |
| Total formula weight | 25550.36 |
| Authors | Huang, P.,Summers, B.J.,Xiong, Y. (deposition date: 2019-04-19, release date: 2019-08-21, Last modification date: 2024-11-20) |
| Primary citation | Huang, P.T.,Summers, B.J.,Xu, C.,Perilla, J.R.,Malikov, V.,Naghavi, M.H.,Xiong, Y. FEZ1 Is Recruited to a Conserved Cofactor Site on Capsid to Promote HIV-1 Trafficking. Cell Rep, 28:2373-, 2019 Cited by PubMed Abstract: HIV-1 uses the microtubule network to traffic the viral capsid core toward the nucleus. Viral nuclear trafficking and infectivity require the kinesin-1 adaptor protein FEZ1. Here, we demonstrate that FEZ1 directly interacts with the HIV-1 capsid and specifically binds capsid protein (CA) hexamers. FEZ1 contains multiple acidic, poly-glutamate stretches that interact with the positively charged central pore of CA hexamers. The FEZ1-capsid interaction directly competes with nucleotides and inositol hexaphosphate (IP6) that bind at the same location. In addition, all-atom molecular dynamic (MD) simulations establish the molecular details of FEZ1-capsid interactions. Functionally, mutation of the FEZ1 capsid-interacting residues significantly reduces trafficking of HIV-1 particles toward the nucleus and early infection. These findings support a model in which the central capsid hexamer pore is a general HIV-1 cofactor-binding hub and FEZ1 serves as a unique CA hexamer pattern sensor to recognize this site and promote capsid trafficking in the cell. PubMed: 31422020DOI: 10.1016/j.celrep.2019.07.079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.052 Å) |
Structure validation
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