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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. Expand
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. Expand
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 theExpand
Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops
  • Young Do Kwon, A. Finzi, +15 authors P. Kwong
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences
  • 26 March 2012
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. Expand
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. Expand
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. Expand
Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G
Crystallized fully glycosylated Env trimers from clades A, B, and G reveal a diversity in oligosaccharide affinity and a requirement for accommodating glycans among known broadly neutralizing antibodies that target the glycan-shielded trimer. Expand
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 byExpand
Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
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. Expand
The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV
It is unambiguously demonstrated that CVN recognizes and binds to the disaccharide Manalpha1 --> 2Manalpha via two distinct binding sites of differing affinities located on opposite ends of the protein. Expand