2B4C

Crystal structure of HIV-1 JR-FL gp120 core protein containing the third variable region (V3) complexed with CD4 and the X5 antibody

Summary for 2B4C

• Entry DOI: 10.2210/pdb2b4c/pdb
• Descriptor: envelope glycoprotein, T-cell surface glycoprotein CD4, anti-HIV-1 gp120 immunoglobulin X5 light chain, ... (8 entities in total)
• Functional Keywords: hiv-1, gp120, jrfl, v3, x5, cd4 induced antibody, viral protein-immune system complex, viral protein/immune system
• Biological source: Human immunodeficiency virus 1; More
• Total number of polymer chains: 4
• Total formula weight: 108808.79

Authors

Huang, C.,Tang, M.,Zhang, M.Y.,Majeed, S.,Montabana, E.,Stanfield, R.L.,Dimitrov, D.S.,Korber, B.,Sodroski, J.,Wilson, I.A.,Wyatt, R.,Kwong, P.D. (deposition date: 2005-09-23, release date: 2005-11-15, Last modification date: 2024-10-16)

Primary citation

Huang, C.C.,Tang, M.,Zhang, M.Y.,Majeed, S.,Montabana, E.,Stanfield, R.L.,Dimitrov, D.S.,Korber, B.,Sodroski, J.,Wilson, I.A.,Wyatt, R.,Kwong, P.D.
Structure of a V3-containing HIV-1 gp120 core.
Science, 310:1025-1028, 2005

PubMed Abstract: The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is immunodominant and contains features essential for coreceptor binding. We determined the structure of V3 in the context of an HIV-1 gp120 core complexed to the CD4 receptor and to the X5 antibody at 3.5 angstrom resolution. Binding of gp120 to cell-surface CD4 would position V3 so that its coreceptor-binding tip protrudes 30 angstroms from the core toward the target cell membrane. The extended nature and antibody accessibility of V3 explain its immunodominance. Together, the results provide a structural rationale for the role of V3 in HIV entry and neutralization.

PubMed: 16284180
DOI: 10.1126/science.1118398

Experimental method

X-RAY DIFFRACTION (3.3 Å)