7TW3

Cryo-EM structure of human ankyrin complex (B2P1A1) from red blood cell

7TW3 の概要

• エントリーDOI: 10.2210/pdb7tw3/pdb
• 関連するPDBエントリー: 7TVZ 7TW0 7TW1 7TW2
• EMDBエントリー: 26142 26143 26144 26145 26146 26147 26148 26149
• 分子名称: Band 3 anion transport protein, Protein 4.2, Ankyrin-1 (3 entities in total)
• 機能のキーワード: red blood cell, ankyrin complex, membrane protein, band 3, protein 4.2
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 487387.26

構造登録者

Xia, X.,Liu, S.H.,Zhou, Z.H. (登録日: 2022-02-06, 公開日: 2022-06-08, 最終更新日: 2024-02-21)

主引用文献

Xia, X.,Liu, S.,Zhou, Z.H.
Structure, dynamics and assembly of the ankyrin complex on human red blood cell membrane.
Nat.Struct.Mol.Biol., 29:698-705, 2022

PubMed Abstract: The cytoskeleton of a red blood cell (RBC) is anchored to the cell membrane by the ankyrin complex. This complex is assembled during RBC genesis and comprises primarily band 3, protein 4.2 and ankyrin, whose mutations contribute to numerous human inherited diseases. High-resolution structures of the ankyrin complex have been long sought-after to understand its assembly and disease-causing mutations. Here, we analyzed native complexes on the human RBC membrane by stepwise fractionation. Cryo-electron microscopy structures of nine band-3-associated complexes reveal that protein 4.2 stabilizes the cytoplasmic domain of band 3 dimer. In turn, the superhelix-shaped ankyrin binds to this protein 4.2 via ankyrin repeats (ARs) 6-13 and to another band 3 dimer via ARs 17-20, bridging two band 3 dimers in the ankyrin complex. Integration of these structures with both prior data and our biochemical data supports a model of ankyrin complex assembly during erythropoiesis and identifies interactions essential for the mechanical stability of RBC.

PubMed: 35655099
DOI: 10.1038/s41594-022-00779-7

実験手法

ELECTRON MICROSCOPY (4.4 Å)