5ACO: Cryo-em Structure Of Pgt128 Fab In Complex With Bg505 Sosip. 664 Env Trimer

Citation:
Abstract
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 A 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.
PDB ID: 5ACODownload
MMDB ID: 133121
PDB Deposition Date: 2015/8/17
Updated in MMDB: 2015/10
Experimental Method:
electron microscopy
Resolution: 4.36  Å
Source Organism:
Human immunodeficiency virus 1
Similar Structures:
Biological Unit for 5ACO: dodecameric; determined by software (PISA)
Molecular Components in 5ACO
Label Count Molecule
Proteins (12 molecules)
3
Hiv-1 Envelope Glycoprotein
Molecule annotation
3
Hiv-1 Envelope Glycoprotein
Molecule annotation
3
Pgt128 FAB
Molecule annotation
3
Pgt128 FAB
Molecule annotation
Chemicals (192 molecules)
1
111
2
30
3
51
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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