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7LFB

Fab 7D6 bound to ApoL1 NTD

Summary for 7LFB
Entry DOI10.2210/pdb7lfb/pdb
DescriptorFab 7D6 heavy chain, Fab 7D6 light chain, Apolipoprotein L1, ... (7 entities in total)
Functional Keywordscomplex, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight63237.36
Authors
Ultsch, M.,Kirchhofer, D. (deposition date: 2021-01-16, release date: 2021-08-04, Last modification date: 2024-11-13)
Primary citationUltsch, 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: 34316015
DOI: 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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