2QAD
Structure of tyrosine-sulfated 412d antibody complexed with HIV-1 YU2 gp120 and CD4
Summary for 2QAD
Entry DOI | 10.2210/pdb2qad/pdb |
Descriptor | Envelope glycoprotein gp160, T-cell surface glycoprotein CD4, anti-HIV-1 antibody 412d light chain, ... (7 entities in total) |
Functional Keywords | viral protein/immune system, viral protein-immune system complex |
Biological source | Human immunodeficiency virus 1 More |
Total number of polymer chains | 8 |
Total formula weight | 216737.58 |
Authors | Huang, C.-C.,Tang, M.,Robinson, J.,Wyatt, R.,Kwong, P.D. (deposition date: 2007-06-14, release date: 2007-09-25, Last modification date: 2024-11-20) |
Primary citation | Huang, C.-C.,Lam, S.N.,Acharya, P.,Tang, M.,Xiang, S.-H.,Hussan, S.S.,Stanfield, R.L.,Robinson, J.,Sodroski, J.,Wilson, I.A.,Wyatt, R.,Bewley, C.A.,Kwong, P.D. Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4 Science, 317:1930-1934, 2007 Cited by PubMed Abstract: 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 (alpha-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. PubMed: 17901336DOI: 10.1126/science.1145373 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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