8SG7
Adeno-Associated Virus Bat origin capsid protein basic regions in complex with importin-alpha 2
Summary for 8SG7
| Entry DOI | 10.2210/pdb8sg7/pdb |
| Descriptor | Importin subunit alpha-1, VP1 capsid (3 entities in total) |
| Functional Keywords | importin, alpha, adeno associated, complex, basic regions, transport, nucleus, transport protein |
| Biological source | Mus musculus (mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 61523.60 |
| Authors | Hoad, M.,Forwood, J.K. (deposition date: 2023-04-11, release date: 2023-07-19, Last modification date: 2024-03-20) |
| Primary citation | Hoad, M.,Roby, J.A.,Forwood, J.K. Structural basis for nuclear import of bat adeno-associated virus capsid protein. J.Gen.Virol., 105:-, 2024 Cited by PubMed Abstract: Adeno-associated viruses (AAV) are one of the world's most promising gene therapy vectors and as a result, are one of the most intensively studied viral vectors. Despite a wealth of research into these vectors, the precise characterisation of AAVs to translocate into the host cell nucleus remains unclear. Recently we identified the nuclear localization signals of an AAV porcine strain and determined its mechanism of binding to host importin proteins. To expand our understanding of diverse AAV import mechanisms we sought to determine the mechanism in which the Cap protein from a bat-infecting AAV can interact with transport receptor importins for translocation into the nucleus. Using a high-resolution crystal structure and quantitative assays, we were able to not only determine the exact region and residues of the N-terminal domain of the Cap protein which constitute the functional NLS for binding with the importin alpha two protein, but also reveal the differences in binding affinity across the importin-alpha isoforms. Collectively our results allow for a detailed molecular view of the way AAV Cap proteins interact with host proteins for localization into the cell nucleus. PubMed: 38441555DOI: 10.1099/jgv.0.001960 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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