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3NZ8

Crystal structure of the HIV-2 neutralizing Fab fragment 7C8

Summary for 3NZ8
Entry DOI10.2210/pdb3nz8/pdb
DescriptorMouse anti V3 antibody 7C8 Fab, heavy chain, Mouse anti V3 antibody 7C8 Fab, light chain, GLYCEROL, ... (4 entities in total)
Functional Keywordsantigen binding, antibody, fab, immunological, hiv-2, v3, gp125, immune system
Biological sourceMus musculus (mouse)
More
Total number of polymer chains4
Total formula weight95858.79
Authors
Uchtenhagen, H.,Friemann, R.,Raszewski, G.,Spetz, A.-L.,Nilsson, L.,Achour, A. (deposition date: 2010-07-16, release date: 2011-05-18, Last modification date: 2024-11-06)
Primary citationUchtenhagen, H.,Friemann, R.,Raszewski, G.,Spetz, A.L.,Nilsson, L.,Achour, A.
Crystal Structure of the HIV-2 Neutralizing Fab Fragment 7C8 with High Specificity to the V3 Region of gp125.
Plos One, 6:e18767-e18767, 2011
Cited by
PubMed Abstract: 7C8 is a mouse monoclonal antibody specific for the third hypervariable region (V3) of the human immunodeficiency virus type 2 (HIV-2)-associated protein gp125. The three-dimensional crystal structure of the Fab fragment of 7C8, determined to 2.7 Å resolution, reveals a deep and narrow antigen-binding cleft with architecture appropriate for an elongated epitope. The highly hydrophobic cleft is bordered on one side by the negatively charged second complementarity determining region (CDR2) and the unusually long positively charged CDR3 of the heavy chain and, on the other side, by the CDR1 of the light chain. Analysis of 7C8 in complex with molecular models of monomeric and trimeric gp125 highlights the importance of a conserved stretch of residues FHSQ that is localized centrally on the V3 region of gp125. Furthermore, modeling also indicates that the Fab fragment neutralizes the virus by sterically impairing subsequent engagement of the gp125 trimer with the co-receptor on the target cell.
PubMed: 21541316
DOI: 10.1371/journal.pone.0018767
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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