7LFB
Fab 7D6 bound to ApoL1 NTD
Summary for 7LFB
| Entry DOI | 10.2210/pdb7lfb/pdb |
| Descriptor | Fab 7D6 heavy chain, Fab 7D6 light chain, Apolipoprotein L1, ... (7 entities in total) |
| Functional Keywords | complex, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 63237.36 |
| Authors | Ultsch, M.,Kirchhofer, D. (deposition date: 2021-01-16, release date: 2021-08-04, Last modification date: 2024-11-13) |
| Primary citation | Ultsch, M.,Holliday, M.J.,Gerhardy, S.,Moran, P.,Scales, S.J.,Gupta, N.,Oltrabella, F.,Chiu, C.,Fairbrother, W.,Eigenbrot, C.,Kirchhofer, D. Structures of the ApoL1 and ApoL2 N-terminal domains reveal a non-classical four-helix bundle motif. Commun Biol, 4:916-916, 2021 Cited by PubMed Abstract: Apolipoprotein L1 (ApoL1) is a circulating innate immunity protein protecting against trypanosome infection. However, two ApoL1 coding variants are associated with a highly increased risk of chronic kidney disease. Here we present X-ray and NMR structures of the N-terminal domain (NTD) of ApoL1 and of its closest relative ApoL2. In both proteins, four of the five NTD helices form a four-helix core structure which is different from the classical four-helix bundle and from the pore-forming domain of colicin A. The reactivity with a conformation-specific antibody and structural models predict that this four-helix motif is also present in the NTDs of ApoL3 and ApoL4, suggesting related functions within the small ApoL family. The long helix 5 of ApoL1 is conformationally flexible and contains the BH3-like region. This BH3-like α-helix resembles true BH3 domains only in sequence and structure but not in function, since it does not bind to the pro-survival members of the Bcl-2 family, suggesting a Bcl-2-independent role in cytotoxicity. These findings should expedite a more comprehensive structural and functional understanding of the ApoL immune protein family. PubMed: 34316015DOI: 10.1038/s42003-021-02387-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.913 Å) |
Structure validation
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