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Crystal structure of the anion exchanger domain of human erythrocyte band 3
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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, Kobayashi, Takuya, Hamasaki, Naotaka and Iwata, So (2015) Crystal structure of the anion exchanger domain of human erythrocyte band 3. Science, 350 (6261). pp. 680-684. doi:10.1126/science.aaa4335 ISSN 0036-8075.
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Official URL: http://dx.doi.org/10.1126/science.aaa4335
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.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QP Physiology | ||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||
Library of Congress Subject Headings (LCSH): | Crystallography, Anions, Bicarbonate ions, Erythrocytes | ||||||||
Journal or Publication Title: | Science | ||||||||
Publisher: | American Association for the Advancement of Science | ||||||||
ISSN: | 0036-8075 | ||||||||
Official Date: | 6 November 2015 | ||||||||
Dates: |
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Volume: | 350 | ||||||||
Number: | 6261 | ||||||||
Number of Pages: | 5 | ||||||||
Page Range: | pp. 680-684 | ||||||||
DOI: | 10.1126/science.aaa4335 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||
Date of first compliant deposit: | 31 December 2015 | ||||||||
Date of first compliant Open Access: | 31 December 2015 | ||||||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Kagaku Gijutsu Shinkō Kikō [Japan Science and Technology Agency] (JST), Japan. Monbu Kagakushō (MEXT), Nihon Gakujutsu Shinkōkai [Japan Society for the Promotion of Science] (NGS), European Union (EU), Wellcome Trust (London, England) | ||||||||
Grant number: | BB/G023425/1 (BBSRC), BB/D019516/1 (BBSRC), 20370035 (NGS), 23370049 (NGS), 201924 (EU), WT089809 (WT) |
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