Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
The structure of V1/V2 in complex with PG9 is reported, identifying a paradigm of antibody recognition for highly glycosylated antigens, which—with PG9—involves a site of vulnerability comprising just two glycans and a strand.
Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4
A framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry is provided and a conserved site on gp120 is defined, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system.
The solution structure of an HMG-I(Y)–DNA complex defines a new architectural minor groove binding motif
The solution structure of a complex between a truncated form of HMG-I(Y), consisting of the second and third DNA binding domains (residues 51–90), and a DNA dodecamer containing the PRDII site of the…
Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G
Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops
The results suggest that the CD4-bound conformation represents a “ground state” for the gp120 core, with variable loop and quaternary interactions restraining unliganded gp120 from “snapping” into this conformation.
Structural basis for diverse N-glycan recognition by HIV-1–neutralizing V1–V2–directed antibody PG16
The structure of antibody PG16 bound to a scaffolded V1–V2 is reported, showing an epitope comprising both high mannose–type and complex-type N-linked glycans, and can provide clues to guide the design of modified antibodies with enhanced neutralization.
Minor groove-binding architectural proteins: structure, function, and DNA recognition.
The structural features of these complexes and the roles they play in facilitating assembly of higher-order protein-DNA complexes are reviewed and elements that contribute to sequence-specific recognition and conformational changes are discussed.
Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
- J. R. Huth, C. Bewley, G. Clore, A. Gronenborn, B. M. Jackson, A. Hinnebusch
- BiologyProtein Science
- 1 November 1997
Several examples are presented that demonstrate the usefulness of this technique for screening protein/DNA complexes, as well as for probing ligand‐receptor interactions, using 15N‐labeled GB1‐peptide fusions and unlabeled target.
Solution structure of cyanovirin-N, a potent HIV-inactivating protein
The solution structure of cyanovirin-N, a potent 11,000 M r HIV-inactivating protein that binds with high affinity and specificity to the HIV surface envelope protein gp120, has been solved by…
Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion.
- A. Plaza, E. Gustchina, Heather L. Baker, M. Kelly, C. Bewley
- Chemistry, BiologyJournal of Natural Products
- 27 October 2007
Four new cyclic depsipeptides termed mirabamides A-D (1-4) have been isolated from the marine sponge Siliquariaspongia mirabilis and shown to potently inhibit HIV-1 fusion and demonstrate that these peptides can act at the early stages of HIV- 1 entry.