3SE8
Crystal structure of broadly and potently neutralizing antibody VRC03 in complex with HIV-1 gp120
Summary for 3SE8
| Entry DOI | 10.2210/pdb3se8/pdb |
| Related | 3NGB |
| Descriptor | HIV-1 Clade AE strain 93TH057 gp120, Heavy chain of antibody VRC03, Light chain of antibody VRC03, ... (8 entities in total) |
| Functional Keywords | hiv, gp120, antibody, vrc03, neutralization, vaccine, envelope glycoprotein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Human immunodeficiency virus 1 More |
| Total number of polymer chains | 3 |
| Total formula weight | 91100.82 |
| Authors | Kwong, P.D.,Zhou, T. (deposition date: 2011-06-10, release date: 2011-08-10, Last modification date: 2024-11-27) |
| Primary citation | Wu, X.,Zhou, T.,Zhu, J.,Zhang, B.,Georgiev, I.,Wang, C.,Chen, X.,Longo, N.S.,Louder, M.,McKee, K.,O'Dell, S.,Perfetto, S.,Schmidt, S.D.,Shi, W.,Wu, L.,Yang, Y.,Yang, Z.Y.,Yang, Z.,Zhang, Z.,Bonsignori, M.,Crump, J.A.,Kapiga, S.H.,Sam, N.E.,Haynes, B.F.,Simek, M.,Burton, D.R.,Koff, W.C.,Doria-Rose, N.A.,Connors, M.,Mullikin, J.C.,Nabel, G.J.,Roederer, M.,Shapiro, L.,Kwong, P.D.,Mascola, J.R. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science, 333:1593-1602, 2011 Cited by PubMed Abstract: Antibody VRC01 is a human immunoglobulin that neutralizes about 90% of HIV-1 isolates. To understand how such broadly neutralizing antibodies develop, we used x-ray crystallography and 454 pyrosequencing to characterize additional VRC01-like antibodies from HIV-1-infected individuals. Crystal structures revealed a convergent mode of binding for diverse antibodies to the same CD4-binding-site epitope. A functional genomics analysis of expressed heavy and light chains revealed common pathways of antibody-heavy chain maturation, confined to the IGHV1-2*02 lineage, involving dozens of somatic changes, and capable of pairing with different light chains. Broadly neutralizing HIV-1 immunity associated with VRC01-like antibodies thus involves the evolution of antibodies to a highly affinity-matured state required to recognize an invariant viral structure, with lineages defined from thousands of sequences providing a genetic roadmap of their development. PubMed: 21835983DOI: 10.1126/science.1207532 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.895 Å) |
Structure validation
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