6OMT
HIV-1 capsid hexamer R18D mutant
6OMT の概要
| エントリーDOI | 10.2210/pdb6omt/pdb |
| 分子名称 | Capsid protein (2 entities in total) |
| 機能のキーワード | hiv-1, capsid, ca, viral protein |
| 由来する生物種 | Human immunodeficiency virus 1 (HIV-1) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 25550.36 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.052 Å) |
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