期刊
STRUCTURE
卷 26, 期 4, 页码 619-+出版社
CELL PRESS
DOI: 10.1016/j.str.2018.02.014
关键词
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资金
- NCRR NIH HHS [S10 RR023057] Funding Source: Medline
- NIAID NIH HHS [R01 AI043203, R01 AI094386, R21 AI106528] Funding Source: Medline
- NIDCR NIH HHS [R01 DE025567] Funding Source: Medline
- NIGMS NIH HHS [U24 GM116792, R01 GM071940] Funding Source: Medline
- NIH HHS [S10 OD018111] Funding Source: Medline
Prior crystal structures of the vault have provided clues of its structural variability but are non-conclusive due to crystal packing. Here, we obtained vaults by engineering at the N terminus of rat major vault protein (MVP) an HIV-1 Gag protein segment and determined their near-atomic resolution (similar to 4.8 A degrees) structures in a solution/non-crystalline environment. The barrel-shaped vaults in solution adopt two conformations, 1 and 2, both with D39 symmetry. From the N to C termini, each MVP monomer has three regions: body, shoulder, and cap. While conformation 1 is identical to one of the crystal structures, the shoulder in conformation 2 is translocated longitudinally up to 10 angstrom, resulting in an outward-projected cap. Our structures clarify the structural discrepancies in the body region in the prior crystal-lography models. The vault's drug-delivery potential is highlighted by the internal disposition and structural flexibility of its Gag-loaded N-terminal extension at the barrel waist of the engineered vault.
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