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

Author:

Arakawa Takatoshi123,Kobayashi-Yurugi Takami13,Alguel Yilmaz456,Iwanari Hiroko7,Hatae Hinako8,Iwata Momi45,Abe Yoshito9,Hino Tomoya13,Ikeda-Suno Chiyo123,Kuma Hiroyuki8,Kang Dongchon10,Murata Takeshi1311,Hamakubo Takao7,Cameron Alexander D.145612,Kobayashi Takuya12313,Hamasaki Naotaka8,Iwata So12345

Affiliation:

1. Japan Science and Technology Agency (JST), Exploratory Research for Advanced Technology (ERATO) Human Receptor Crystallography Project, Konoe-cho, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.

2. JST, Research Acceleration Program, Membrane Protein Crystallography Project, Konoe-cho, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.

3. Department of Cell Biology, Kyoto University Faculty of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.

4. Division of Molecular Biosciences, Membrane Protein Crystallography group, Imperial College London, London SW7 2AZ, UK.

5. Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Chilton, Oxfordshire OX11 0DE, UK.

6. Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell Oxford, Didcot, Oxfordshire OX11 0FA, UK.

7. Department of Quantitative Biology and Medicine, Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo 153-8904, Japan.

8. Faculty of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch-cho, Sasebo, Nagasaki 859-3298, Japan.

9. Department of Protein Structure, Function and Design, Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.

10. Department of Clinical Chemistry and Laboratory Medicine, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan.

11. Department of Chemistry, Graduate School of Science, Chiba University, 1-33 Yayoi-cho, Inage, Chiba 263-8522, Japan.

12. School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK.

13. Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.

Abstract

Getting rid of carbon dioxide In mammals, red blood cells deliver oxygen to tissues and remove carbon dioxide. Key to this essential process is a membrane protein called anion exchanger 1 (AE1) which transports bicarbonate (formed from carbon dioxide) out of red blood cells in exchange for chloride. This decreases the pH inside the blood cells, so that oxygen is released from hemoglobin and can diffuse into tissues. Arakawa et al. report the crystal structure of the transmembrane anion exchanger domain of AE1, which includes 14 transmembrane helices. The structure provides a basis for understanding the effects of mutations that lead to red blood cell diseases and also gives insight into the mechanism of ion transport. Science , this issue p. 680

Funder

Wellcome Trust

Biotechnology and Biological Sciences Research Council

Ministry of Education, Culture, Sports, Science, and Technology, Japan (MEXT)

Grant-in-Aid for Scientific Research

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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