1GGI
CRYSTAL STRUCTURE OF AN HIV-1 NEUTRALIZING ANTIBODY 50.1 IN COMPLEX WITH ITS V3 LOOP PEPTIDE ANTIGEN
Summary for 1GGI
| Entry DOI | 10.2210/pdb1ggi/pdb |
| Descriptor | IGG2A 50.1 FAB (LIGHT CHAIN), IGG2A 50.1 FAB (HEAVY CHAIN), HIV-1 V3 LOOP PEPTIDE ANTIGEN (3 entities in total) |
| Functional Keywords | immunoglobulin |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 6 |
| Total formula weight | 99300.65 |
| Authors | Stanfield, R.L.,Rini, J.M.,Wilson, I.A. (deposition date: 1993-04-02, release date: 1993-10-31, Last modification date: 2024-10-16) |
| Primary citation | Rini, J.M.,Stanfield, R.L.,Stura, E.A.,Salinas, P.A.,Profy, A.T.,Wilson, I.A. Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen. Proc.Natl.Acad.Sci.USA, 90:6325-6329, 1993 Cited by PubMed Abstract: The crystal structure of the Fab fragment of a human immunodeficiency virus type 1 (HIV-1) neutralizing monoclonal antibody Fab has been determined at 2.8 A resolution in complex with a linear 16-residue peptide from the third hypervariable region (V3) of gp120. The first 9 residues of the peptide are ordered in the electron density maps, and their conformation is in partial agreement with the beta-strand-type II beta-turn structure predicted for this portion of the V3 loop. Notably, several of the peptide residues that are well conserved among different HIV-1 isolates contact a nonpolar 25-A-long groove in the antibody-combining site. The largely extended structure of the peptide differs from the beta-turns seen as the primary determinants in other published anti-peptide Fab structures. Analysis of the specific Fab-peptide interactions only partially explains the MN isolate specificity shown by this antibody. PubMed: 8327513DOI: 10.1073/pnas.90.13.6325 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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