View source for 5a16


==Crystal structure of Fab4201 raised against Human Erythrocyte Anion Exchanger 1==
<StructureSection load='5a16' size='340' side='right'caption='[[5a16]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5a16]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A16 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a16 OCA], [https://pdbe.org/5a16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a16 RCSB], [https://www.ebi.ac.uk/pdbsum/5a16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a16 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3KL48_MOUSE A0A0M3KL48_MOUSE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 (AE1(CTD)) 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 AE1(CTD), and to propose a possible transport mechanism that could explain why selected mutations lead to disease.

Crystal structure of the anion exchanger domain of human erythrocyte band 3.,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 Science. 2015 Nov 6;350(6261):680-4. doi: 10.1126/science.aaa4335. PMID:26542571<ref>PMID:26542571</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5a16" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Abe Y]]
[[Category: Alguel Y]]
[[Category: Arakawa T]]
[[Category: Cameron A]]
[[Category: Hamakubo T]]
[[Category: Hamasaki N]]
[[Category: Hatae H]]
[[Category: Hino T]]
[[Category: Ikeda-Suno C]]
[[Category: Iwanari H]]
[[Category: Iwata M]]
[[Category: Iwata S]]
[[Category: Kang D]]
[[Category: Kobayashi T]]
[[Category: Kobayashi-Yugiri T]]
[[Category: Kuma H]]
[[Category: Murata T]]
[[Category: Weyand S]]