4XBE
Crystal structure of human 4E10 Fab in complex with its peptide epitope on HIV-1 gp41: crystals cryoprotected with sphingomyelin (02:0 SM (d18:1/2:0)).
Summary for 4XBE
| Entry DOI | 10.2210/pdb4xbe/pdb |
| Related | 2FX7 4XAW 4XBG 4XBP 4XC1 4XC3 4XCC 4XCE 4XCF 4XCN 4XCY |
| Descriptor | 4E10 FAB LIGHT CHAIN, 4E10 Fab heavy chain, PEPTIDE FRAGMENT OF HIV GLYCOPROTEIN (GP41) including the region 671-683 of the MPER, ... (5 entities in total) |
| Functional Keywords | hiv-1 gp41 mper, 4e10 fab, membrane lipid, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 49634.50 |
| Authors | Irimia, A.,Stanfield, R.L.,Wilson, I.A. (deposition date: 2014-12-16, release date: 2016-02-03, Last modification date: 2024-11-06) |
| Primary citation | Irimia, A.,Sarkar, A.,Stanfield, R.L.,Wilson, I.A. Crystallographic Identification of Lipid as an Integral Component of the Epitope of HIV Broadly Neutralizing Antibody 4E10. Immunity, 44:21-31, 2016 Cited by PubMed Abstract: Numerous studies of the anti-HIV-1 envelope glycoprotein 41 (gp41) broadly neutralizing antibody 4E10 suggest that 4E10 also interacts with membrane lipids, but the antibody regions contacting lipids and its orientation with respect to the viral membrane are unknown. Vaccine immunogens capable of re-eliciting these membrane proximal external region (MPER)-like antibodies may require a lipid component to be successful. We performed a systematic crystallographic study of lipid binding to 4E10 to identify lipids bound by the antibody and the lipid-interacting regions. We identified phosphatidic acid, phosphatidylglycerol, and glycerol phosphate as specific ligands for 4E10 in the crystal structures. 4E10 used its CDRH1 loop to bind the lipid head groups, while its CDRH3 interacted with the hydrophobic lipid tails. Identification of the lipid binding sites on 4E10 may aid design of immunogens for vaccines that include a lipid component in addition to the MPER on gp41 for generation of broadly neutralizing antibodies. PubMed: 26777395DOI: 10.1016/j.immuni.2015.12.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.756 Å) |
Structure validation
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