7V07

Band 3-I-TM local refinement from erythrocyte ankyrin-1 complex consensus reconstruction

7V07 の概要

• エントリーDOI: 10.2210/pdb7v07/pdb
• EMDBエントリー: 26874 26886 26916 26917 26918 26919 26940 26943 26944 26948 26949 26950 26951 26952 26953 26954 26955 26956 26958 26960 26965 26972 26973 26974 26975 26978 26979 26982 26988
• 分子名称: Glycophorin-A, Band 3 anion transport protein, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-4)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: membrane protein, anion exchange, erythrocyte, glycoprotein, transport protein
• 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: 242863.93

構造登録者

Vallese, F.,Kim, K.,Yen, L.Y.,Johnston, J.D.,Noble, A.J.,Cali, T.,Clarke, O.B. (登録日: 2022-05-10, 公開日: 2022-07-20, 最終更新日: 2024-10-23)

主引用文献

Vallese, F.,Kim, K.,Yen, L.Y.,Johnston, J.D.,Noble, A.J.,Cali, T.,Clarke, O.B.
Architecture of the human erythrocyte ankyrin-1 complex.
Nat.Struct.Mol.Biol., 29:706-718, 2022

PubMed Abstract: The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2, glycophorin A and glycophorin B. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and, unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering.

PubMed: 35835865
DOI: 10.1038/s41594-022-00792-w

実験手法

ELECTRON MICROSCOPY (2.8 Å)