Science (American Association for the Advancement of Science), 2007-09, Vol.317 (5846), p.1930-1934
2007
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- Autor(en) / Beteiligte
- Titel
- Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4
- Ist Teil von
- Science (American Association for the Advancement of Science), 2007-09, Vol.317 (5846), p.1930-1934
- Ort / Verlag
- Washington, DC: American Association for the Advancement of Science
- Erscheinungsjahr
- 2007
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.1145373Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2278242
- Format
- –
- Schlagworte
- AIDS, Amino Acid Sequence, Antibodies, Binding sites, Biological and medical sciences, Biomedical research, CD4 Antigens - chemistry, CD4 Antigens - immunology, Cellular biology, Crystal structure, Crystallography, X-Ray, Crystals, Fundamental and applied biological sciences. Psychology, Glycoproteins, HIV, HIV 1, HIV Antibodies - chemistry, HIV Antibodies - immunology, HIV Envelope Protein gp120 - chemistry, HIV Envelope Protein gp120 - immunology, HIV Envelope Protein gp120 - metabolism, HIV-1 - metabolism, Human immunodeficiency virus, Human immunodeficiency virus 1, Humans, Hydrogen bonds, Immunology, Models, Molecular, Molecular biophysics, Molecular Mimicry, Molecular Sequence Data, Molecular structure, Nuclear magnetic resonance, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments - chemistry, Peptide Fragments - metabolism, Receptors, Receptors, CCR5 - chemistry, Receptors, CCR5 - metabolism, Structure in molecular biology, Sulfates, Sulfates - metabolism, Tridimensional structure, Tyrosine - metabolism, Virus Internalization