Anion exchanger 1 (AE1), also known as band 3 or SLC4A1 or Band 3 anion transport protein exchanges chloride and bicarbonate across the red blood cell membrane, assisting in removing carbon dioxide from tissues. It also anchors the membrane skeleton [1]. Band 3's name comes from its appearance as the third major band on SDS-PAGE of red blood cell membrane proteins [2].
Its function has been studied for more than 150 years; even so, the first complete structure was not published until 2015 [3], and the first crystals grown without addition of an antibody were grown on the International Space Station [4].
Structural highlights
Band 3 functions as a dimer. Each monomer contains fourteen transmembrane segments, as well as an intracellular domain that plays a gating role and a small extracellular domain.
- ↑ Jennings ML. Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1. Am J Physiol Cell Physiol. 2021 Dec 1;321(6):C1028-C1059. PMID:34669510 doi:10.1152/ajpcell.00275.2021
- ↑ Fairbanks G, Steck TL, Wallach DF. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606-17. PMID:4326772 doi:10.1021/bi00789a030
- ↑ 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. Crystal structure of the anion exchanger domain of human erythrocyte band 3. Science. 2015 Nov 6;350(6261):680-4. doi: 10.1126/science.aaa4335. PMID:26542571 doi:https://dx.doi.org/10.1126/science.aaa4335
- ↑ Hatae H, Inaka K, Okamura R, Furubayashi N, Kamo M, Kobayashi T, Abe Y, Iwata S, Hamasaki N. Crystallization of Human Erythrocyte Band 3, the anion exchanger, at the International Space Station "KIBO". Anal Biochem. 2018 Oct 15;559:91-93. PMID:30118660 doi:10.1016/j.ab.2018.08.009
