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4JO3

Crystal structure of rabbit mAb R20 Fab in complex with V3 C-terminus of HIV-1 Consensus B gp120

Summary for 4JO3
Entry DOI10.2210/pdb4jo3/pdb
Related4JO1 4JO2 4JO4
Descriptormonoclonal anti-HIV-1 gp120 V3 antibody R20 light chain, monoclonal anti-HIV-1 gp120 V3 antibody R20 heavy chain, gp120, ... (5 entities in total)
Functional Keywordsig, antibody, immune system-viral protein complex, immune system/viral protein
Biological sourceOryctolagus cuniculus (rabbit)
More
Cellular locationVirion membrane : Q9YY05
Total number of polymer chains6
Total formula weight96423.12
Authors
Pan, R.M.,Kong, X.P. (deposition date: 2013-03-16, release date: 2013-07-31, Last modification date: 2024-11-27)
Primary citationPan, R.,Sampson, J.M.,Chen, Y.,Vaine, M.,Wang, S.,Lu, S.,Kong, X.P.
Rabbit Anti-HIV-1 Monoclonal Antibodies Raised by Immunization Can Mimic the Antigen-Binding Modes of Antibodies Derived from HIV-1-Infected Humans.
J.Virol., 87:10221-10231, 2013
Cited by
PubMed Abstract: The rabbit is a commonly used animal model in studying antibody responses in HIV/AIDS vaccine development. However, no rabbit monoclonal antibodies (MAbs) have been developed previously to study the epitope-specific antibody responses against HIV-1 envelope (Env) glycoproteins, and little is known about how the rabbit immune system can mimic the human immune system in eliciting such antibodies. Here we present structural analyses of two rabbit MAbs, R56 and R20, against the third variable region (V3) of HIV-1 gp120. R56 recognizes the well-studied immunogenic region in the V3 crown, while R20 targets a less-studied region at the C terminus of V3. By comparison of the Fab/epitope complex structures of these two antibodies raised by immunization with that of the corresponding human antibodies derived from patients chronically infected with HIV-1, we found that rabbit antibodies can recognize immunogenic regions of gp120 and mimic the binding modes of human antibodies. This result can provide new insight into the use of the rabbit as an animal model in AIDS vaccine development.
PubMed: 23864637
DOI: 10.1128/JVI.00843-13
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

238895

数据于2025-07-16公开中

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