期刊
STRUCTURE
卷 23, 期 10, 页码 1943-1951出版社
CELL PRESS
DOI: 10.1016/j.str.2015.07.020
关键词
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资金
- California HIV/AIDS Research Program [D12-SRI-353]
- Leona M. and Harry B. Helmsley Charitable Trust [2012-PG-MED002]
- Scripps CHAVI-ID [UM1 AI100663, P01 AI82362]
- International AIDS Vaccine Initiative
- Bill and Melinda Gates Foundation (CAVD)
Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, which can result in a large number of possible glycoforms. This sample heterogeneity can be problematic for structural studies, particularly X-ray crystallography. Thus, crystal structures of heavily glycosylated proteins such as the HIV-1 Env viral spike protein have been determined by removing the majority of glycans. This step is most frequently carried out using Endoglycosidase H (EndoH) and requires that all expressed glycans be in the high-mannose form, which is often not the native glycoform. With significantly improved technologies in single-particle cryoelectron microscopy, we demonstrate that it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 angstrom resolution. At this resolution we can now analyze the complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in the context of the trimer expressed with native glycans.
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