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

Takatoshi Arakawa, Takami Kobayashi-Yurugi, Yilmaz Alguel, Hiroko Iwanari, Hinako Hatae, Momi Iwata, Yoshito Abe, Tomoya Hino, Chiyo Ikeda-Suno, Hiroyuki Kuma, Dongchon Kang, Takeshi Murata, Takao Hamakubo, Alexander D. Cameron, Takuya Kobayashi, Naotaka Hamasaki, So Iwata

Research output: Contribution to journalArticlepeer-review

179 Citations (Scopus)


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 (AE1CTD) 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 AE1CTD, and to propose a possible transport mechanism that could explain why selected mutations lead to disease.

Original languageEnglish
Pages (from-to)680-684
Number of pages5
Issue number6261
Publication statusPublished - Nov 6 2015

All Science Journal Classification (ASJC) codes

  • General


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