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.
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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 -
