3HI1
Structure of HIV-1 gp120 (core with V3) in Complex with CD4-Binding-Site Antibody F105
Summary for 3HI1
| Entry DOI | 10.2210/pdb3hi1/pdb |
| Descriptor | Glycoprotein 120, F105 Light Chain, F105 Heavy Chain, ... (5 entities in total) |
| Functional Keywords | hiv, gp120, cd4 binding site antibody, f105, immune evasion, aids, apoptosis, cell membrane, cleavage on pair of basic residues, disulfide bond, envelope protein, fusion protein, glycoprotein, host-virus interaction, lipoprotein, membrane, palmitate, transmembrane, viral immunoevasion, virion, structural protein-immune system complex, structural protein/immune system |
| Biological source | Human immunodeficiency virus type 1 (HIV-1) More |
| Total number of polymer chains | 6 |
| Total formula weight | 172578.10 |
| Authors | Kwon, Y.D.,Chen, L.,Zhou, T.,Wu, X.,O'Dell, S.,Cavacini, L.,Hessell, A.J.,Pancera, M.,Tang, M.,Xu, L.,Yang, Z.,Zhang, M.-Y.,Arthos, J.,Burton, D.R.,Dimitrov, D.,Nabel, G.J.,Posner, M.,Sodroski, J.,Wyatt, R.,Mascola, J.R.,Kwong, P.D. (deposition date: 2009-05-18, release date: 2009-11-17, Last modification date: 2024-11-06) |
| Primary citation | Chen, L.,Do Kwon, Y.,Zhou, T.,Wu, X.,O'Dell, S.,Cavacini, L.,Hessell, A.J.,Pancera, M.,Tang, M.,Xu, L.,Yang, Z.Y.,Zhang, M.Y.,Arthos, J.,Burton, D.R.,Dimitrov, D.S.,Nabel, G.J.,Posner, M.R.,Sodroski, J.,Wyatt, R.,Mascola, J.R.,Kwong, P.D. Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science, 326:1123-1127, 2009 Cited by PubMed Abstract: The site on HIV-1 gp120 that binds to the CD4 receptor is vulnerable to antibodies. However, most antibodies that interact with this site cannot neutralize HIV-1. To understand the basis of this resistance, we determined co-crystal structures for two poorly neutralizing, CD4-binding site (CD4BS) antibodies, F105 and b13, in complexes with gp120. Both antibodies exhibited approach angles to gp120 similar to those of CD4 and a rare, broadly neutralizing CD4BS antibody, b12. Slight differences in recognition, however, resulted in substantial differences in F105- and b13-bound conformations relative to b12-bound gp120. Modeling and binding experiments revealed these conformations to be poorly compatible with the viral spike. This incompatibility, the consequence of slight differences in CD4BS recognition, renders HIV-1 resistant to all but the most accurately targeted antibodies. PubMed: 19965434DOI: 10.1126/science.1175868 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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