6bp7

Publication Abstract from PubMed

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 ( approximately 4.8 A) 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 A, resulting in an outward-projected cap. Our structures clarify the structural discrepancies in the body region in the prior crystallography 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.

Solution Structures of Engineered Vault Particles.,Ding K, Zhang X, Mrazek J, Kickhoefer VA, Lai M, Ng HL, Yang OO, Rome LH, Zhou ZH Structure. 2018 Mar 7. pii: S0969-2126(18)30054-6. doi:, 10.1016/j.str.2018.02.014. PMID:29551289^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.