4YZF

Crystal structure of the anion exchanger domain of human erythrocyte Band 3

4YZF の概要

• エントリーDOI: 10.2210/pdb4yzf/pdb
• 分子名称: Band 3 anion transport protein, FAB fragment of Immunoglobulin (IgG) molecule, 2,2'-ethane-1,2-diylbis{5-[(sulfanylmethyl)amino]benzenesulfonic acid}, ... (4 entities in total)
• 機能のキーワード: immune system, human membrane protein, anion exchanger, erythrocytes
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein: P02730
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 601715.14

構造登録者

Alguel, Y.,Arakawa, T.,Yugiri, T.K.,Iwanari, H.,Hatae, H.,Iwata, M.,Abe, Y.,Hino, T.,Suno, C.I.,Kuma, H.,Kang, D.,Murata, T.,Hamakubo, T.,Cameron, A.D.,Kobayashi, T.,Hamasaki, N.,Iwata, S. (登録日: 2015-03-25, 公開日: 2015-11-04, 最終更新日: 2024-10-16)

主引用文献

Arakawa, T.,Kobayashi-Yurugi, T.,Alguel, Y.,Iwanari, H.,Hatae, H.,Iwata, M.,Abe, Y.,Hino, T.,Ikeda-Suno, C.,Kuma, H.,Kang, D.,Murata, T.,Hamakubo, T.,Cameron, A.D.,Kobayashi, T.,Hamasaki, N.,Iwata, S.
Crystal structure of the anion exchanger domain of human erythrocyte band 3.
Science, 350:680-684, 2015

PubMed Abstract: Anion exchanger 1 (AE1), also known as band 3 or SLC4A1, plays a key role in the removal of carbon dioxide from tissues by facilitating the exchange of chloride and bicarbonate across the plasma membrane of erythrocytes. An isoform of AE1 is also present in the kidney. Specific mutations in human AE1 cause several types of hereditary hemolytic anemias and/or distal renal tubular acidosis. Here we report the crystal structure of the band 3 anion exchanger domain (AE1(CTD)) at 3.5 angstroms. The structure is locked in an outward-facing open conformation by an inhibitor. Comparing this structure with a substrate-bound structure of the uracil transporter UraA in an inward-facing conformation allowed us to identify the anion-binding position in the AE1(CTD), and to propose a possible transport mechanism that could explain why selected mutations lead to disease.

PubMed: 26542571
DOI: 10.1126/science.aaa4335

実験手法

X-RAY DIFFRACTION (3.5 Å)