7L6K

ApoL1 N-terminal domain

7L6K の概要

• エントリーDOI: 10.2210/pdb7l6k/pdb
• NMR情報: BMRB: 30832
• 分子名称: Apolipoprotein L1 (1 entity in total)
• 機能のキーワード: ion channel, kidney disease, lipoprotein, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13309.07

構造登録者

Holliday, M.J.,Ultsch, M.,Moran, P.,Fairbrother, W.J.,Kirchhofer, D. (登録日: 2020-12-23, 公開日: 2021-08-04, 最終更新日: 2024-05-15)

主引用文献

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

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

実験手法

SOLUTION NMR