1NAK
IGG1 FAB FRAGMENT (83.1) COMPLEX WITH 16-RESIDUE PEPTIDE (RESIDUES 304-321 OF HIV-1 GP120 (MN ISOLATE))
Summary for 1NAK
| Entry DOI | 10.2210/pdb1nak/pdb |
| Descriptor | Fab 83.1 - light chain, Fab 83.1 - heavy chain, Peptide MP1, ... (4 entities in total) |
| Functional Keywords | immunoglobulin fold, immune system |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 6 |
| Total formula weight | 98147.45 |
| Authors | Stanfield, R.L.,Ghiara, J.B.,Saphire, E.O.,Profy, A.T.,Wilson, I.A. (deposition date: 2002-11-27, release date: 2003-11-18, Last modification date: 2024-10-30) |
| Primary citation | Stanfield, R.L.,Ghiara, J.B.,Ollmann Saphire, E.,Profy, A.T.,Wilson, I.A. Recurring conformation of the human immunodeficiency virus type 1 gp120 V3 loop. Virology, 315:159-173, 2003 Cited by PubMed Abstract: The crystal structure of the human immunodeficiency virus type 1 (HIV-1) neutralizing, murine Fab 83.1 in complex with an HIV-1 gp120 V3 peptide has been determined to 2.57 A resolution. The conformation of the V3 loop peptide in complex with Fab 83.1 is very similar to V3 conformations seen previously with two other neutralizing Fabs, 50.1 and 59.1. The repeated identification of this same V3 conformation in complex with three very different, neutralizing antibodies indicates that it is a highly preferred structure for V3 loops on some strains of the HIV-1 virus. PubMed: 14592768DOI: 10.1016/S0042-6822(03)00525-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.57 Å) |
Structure validation
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