Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4
Copyright policy )Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4
The CCR5 co-receptor binds to the HIV-1 gp120 envelope glycoprotein and facilitates HIV-1 entry into cells. Its N terminus is tyrosine-sulfated, as are many antibodies that react with the co-receptor binding site on gp120. We applied nuclear magnetic resonance and crystallographic techniques to analyze the structure of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 and CD4. The conformations of tyrosine-sulfated regions of CCR5 (α-helix) and 412d (extended loop) are surprisingly different. Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system.
- National Institute of Allergy and Infectious Diseases United States
- Dana-Farber Cancer Institute United States
- National Institutes of Health United States
- Harvard University United States
- National Institute of Health Pakistan
Models, Molecular, Receptors, CCR5, Sulfates, Molecular Mimicry, Molecular Sequence Data, HIV Antibodies, HIV Envelope Protein gp120, Virus Internalization, Crystallography, X-Ray, Peptide Fragments, CD4 Antigens, HIV-1, Humans, Tyrosine, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular
Models, Molecular, Receptors, CCR5, Sulfates, Molecular Mimicry, Molecular Sequence Data, HIV Antibodies, HIV Envelope Protein gp120, Virus Internalization, Crystallography, X-Ray, Peptide Fragments, CD4 Antigens, HIV-1, Humans, Tyrosine, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).376 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 1% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 1% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 1%
Citations provided by BIP!Popularity provided by BIP!