1HZH
CRYSTAL STRUCTURE OF THE INTACT HUMAN IGG B12 WITH BROAD AND POTENT ACTIVITY AGAINST PRIMARY HIV-1 ISOLATES: A TEMPLATE FOR HIV VACCINE DESIGN
Summary for 1HZH
| Entry DOI | 10.2210/pdb1hzh/pdb |
| Descriptor | IMMUNOGLOBULIN HEAVY CHAIN, IMMUNOGLOBULIN LIGHT CHAIN,Uncharacterized protein, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | immunoglobulin, antibody, b12, immune system |
| Biological source | Homo sapiens (human) More |
| Cellular location | Secreted : P0DOX5 |
| Total number of polymer chains | 4 |
| Total formula weight | 151628.99 |
| Authors | Saphire, E.O.,Burton, D.R.,Wilson, I.A. (deposition date: 2001-01-24, release date: 2001-08-15, Last modification date: 2024-11-20) |
| Primary citation | Saphire, E.O.,Parren, P.W.,Pantophlet, R.,Zwick, M.B.,Morris, G.M.,Rudd, P.M.,Dwek, R.A.,Stanfield, R.L.,Burton, D.R.,Wilson, I.A. Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design. Science, 293:1155-1159, 2001 Cited by PubMed Abstract: We present the crystal structure at 2.7 angstrom resolution of the human antibody IgG1 b12. Antibody b12 recognizes the CD4-binding site of human immunodeficiency virus-1 (HIV-1) gp120 and is one of only two known antibodies against gp120 capable of broad and potent neutralization of primary HIV-1 isolates. A key feature of the antibody-combining site is the protruding, finger-like long CDR H3 that can penetrate the recessed CD4-binding site of gp120. A docking model of b12 and gp120 reveals severe structural constraints that explain the extraordinary challenge in eliciting effective neutralizing antibodies similar to b12. The structure, together with mutagenesis studies, provides a rationale for the extensive cross-reactivity of b12 and a valuable framework for the design of HIV-1 vaccines capable of eliciting b12-like activity. PubMed: 11498595DOI: 10.1126/science.1061692 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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