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 journalArticle

83 Citations (Scopus)

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 (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
JournalScience
Volume350
Issue number6261
DOIs
Publication statusPublished - Nov 6 2015

Fingerprint

Erythrocyte Anion Exchange Protein 1
Anions
Erythrocytes
Congenital Hemolytic Anemia
Chloride-Bicarbonate Antiporters
Renal Tubular Acidosis
Mutation
Uracil
Bicarbonates
Carbon Dioxide
Chlorides
Protein Isoforms
Cell Membrane
Kidney

All Science Journal Classification (ASJC) codes

  • General

Cite this

Arakawa, T., Kobayashi-Yurugi, T., Alguel, Y., Iwanari, H., Hatae, H., Iwata, M., ... Iwata, S. (2015). Crystal structure of the anion exchanger domain of human erythrocyte band 3. Science, 350(6261), 680-684. https://doi.org/10.1126/science.aaa4335

Crystal structure of the anion exchanger domain of human erythrocyte band 3. / Arakawa, Takatoshi; Kobayashi-Yurugi, Takami; Alguel, Yilmaz; Iwanari, Hiroko; Hatae, Hinako; Iwata, Momi; Abe, Yoshito; Hino, Tomoya; Ikeda-Suno, Chiyo; Kuma, Hiroyuki; Kang, Dongchon; Murata, Takeshi; Hamakubo, Takao; Cameron, Alexander D.; Kobayashi, Takuya; Hamasaki, Naotaka; Iwata, So.

In: Science, Vol. 350, No. 6261, 06.11.2015, p. 680-684.

Research output: Contribution to journalArticle

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, AD, Kobayashi, T, Hamasaki, N & Iwata, S 2015, 'Crystal structure of the anion exchanger domain of human erythrocyte band 3', Science, vol. 350, no. 6261, pp. 680-684. https://doi.org/10.1126/science.aaa4335
Arakawa T, Kobayashi-Yurugi T, Alguel Y, Iwanari H, Hatae H, Iwata M et al. Crystal structure of the anion exchanger domain of human erythrocyte band 3. Science. 2015 Nov 6;350(6261):680-684. https://doi.org/10.1126/science.aaa4335
Arakawa, Takatoshi ; Kobayashi-Yurugi, Takami ; Alguel, Yilmaz ; Iwanari, Hiroko ; Hatae, Hinako ; Iwata, Momi ; Abe, Yoshito ; Hino, Tomoya ; Ikeda-Suno, Chiyo ; Kuma, Hiroyuki ; Kang, Dongchon ; Murata, Takeshi ; Hamakubo, Takao ; Cameron, Alexander D. ; Kobayashi, Takuya ; Hamasaki, Naotaka ; Iwata, So. / Crystal structure of the anion exchanger domain of human erythrocyte band 3. In: Science. 2015 ; Vol. 350, No. 6261. pp. 680-684.
@article{46e6af6ce11e44a28fcecf9fc08d8c8a,
title = "Crystal structure of the anion exchanger domain of human erythrocyte band 3",
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 (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.",
author = "Takatoshi Arakawa and Takami Kobayashi-Yurugi and Yilmaz Alguel and Hiroko Iwanari and Hinako Hatae and Momi Iwata and Yoshito Abe and Tomoya Hino and Chiyo Ikeda-Suno and Hiroyuki Kuma and Dongchon Kang and Takeshi Murata and Takao Hamakubo and Cameron, {Alexander D.} and Takuya Kobayashi and Naotaka Hamasaki and So Iwata",
year = "2015",
month = "11",
day = "6",
doi = "10.1126/science.aaa4335",
language = "English",
volume = "350",
pages = "680--684",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6261",

}

TY - JOUR

T1 - Crystal structure of the anion exchanger domain of human erythrocyte band 3

AU - Arakawa, Takatoshi

AU - Kobayashi-Yurugi, Takami

AU - Alguel, Yilmaz

AU - Iwanari, Hiroko

AU - Hatae, Hinako

AU - Iwata, Momi

AU - Abe, Yoshito

AU - Hino, Tomoya

AU - Ikeda-Suno, Chiyo

AU - Kuma, Hiroyuki

AU - Kang, Dongchon

AU - Murata, Takeshi

AU - Hamakubo, Takao

AU - Cameron, Alexander D.

AU - Kobayashi, Takuya

AU - Hamasaki, Naotaka

AU - Iwata, So

PY - 2015/11/6

Y1 - 2015/11/6

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84947461476&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84947461476&partnerID=8YFLogxK

U2 - 10.1126/science.aaa4335

DO - 10.1126/science.aaa4335

M3 - Article

C2 - 26542571

AN - SCOPUS:84947461476

VL - 350

SP - 680

EP - 684

JO - Science

JF - Science

SN - 0036-8075

IS - 6261

ER -