6AVN
Crystal structure of unbound anti-HIV antibody Fab PGV19 at 2.5 A
Summary for 6AVN
| Entry DOI | 10.2210/pdb6avn/pdb |
| Descriptor | PGV19 Fab heavy chain, PGV19 Fab light chain, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | vrc01-class lambda antibody, cd4 binding site epitope, immune system, anti-hiv neutralizing antibody |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 2 |
| Total formula weight | 47072.75 |
| Authors | Sarkar, A.,Wilson, I.A. (deposition date: 2017-09-03, release date: 2018-06-27, Last modification date: 2024-10-09) |
| Primary citation | Sarkar, A.,Bale, S.,Behrens, A.J.,Kumar, S.,Sharma, S.K.,de Val, N.,Pallesen, J.,Irimia, A.,Diwanji, D.C.,Stanfield, R.L.,Ward, A.B.,Crispin, M.,Wyatt, R.T.,Wilson, I.A. Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer. Nat Commun, 9:1956-1956, 2018 Cited by PubMed Abstract: Furin cleavage of the HIV envelope glycoprotein is an essential step for cell entry that enables formation of well-folded, native-like glycosylated trimers, releases constraints on the fusion peptide, and limits enzymatic processing of the N-glycan shield. Here, we show that a cleavage-independent, stabilized, soluble Env trimer mimic (BG505 NFL.664) exhibits a "closed-form", native-like, prefusion conformation akin to furin-cleaved Env trimers. The crystal structure of BG505 NFL.664 at 3.39 Å resolution with two potent bNAbs also identifies the full epitopes of PGV19 and PGT122 that target the receptor binding site and N332 supersite, respectively. Quantitative site-specific analysis of the glycan shield reveals that native-like glycan processing is maintained despite furin-independent maturation in the secretory pathway. Thus, cleavage-independent NFL Env trimers exhibit quaternary protein and carbohydrate structures similar to the native viral spike that further validate their potential as vaccine immunogen candidates. PubMed: 29769533DOI: 10.1038/s41467-018-04272-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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