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Structure paper

TitleSubstrate binding and inhibition of the anion exchanger 1 transporter.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 10, Page 1495-1504, Year 2023
Publish dateSep 7, 2023
AuthorsMichael J Capper / Shifan Yang / Alexander C Stone / Sezen Vatansever / Gregory Zilberg / Yamuna Kalyani Mathiharan / Raul Habib / Keino Hutchinson / Yihan Zhao / Avner Schlessinger / Mihaly Mezei / Roman Osman / Bin Zhang / Daniel Wacker /
PubMed AbstractAnion exchanger 1 (AE1), a member of the solute carrier (SLC) family, is the primary bicarbonate transporter in erythrocytes, regulating pH levels and CO transport between lungs and tissues. Previous ...Anion exchanger 1 (AE1), a member of the solute carrier (SLC) family, is the primary bicarbonate transporter in erythrocytes, regulating pH levels and CO transport between lungs and tissues. Previous studies characterized its role in erythrocyte structure and provided insight into transport regulation. However, key questions remain regarding substrate binding and transport, mechanisms of drug inhibition and modulation by membrane components. Here we present seven cryo-EM structures in apo, bicarbonate-bound and inhibitor-bound states. These, combined with uptake and computational studies, reveal important molecular features of substrate recognition and transport, and illuminate sterol binding sites, to elucidate distinct inhibitory mechanisms of research chemicals and prescription drugs. We further probe the substrate binding site via structure-based ligand screening, identifying an AE1 inhibitor. Together, our findings provide insight into mechanisms of solute carrier transport and inhibition.
External linksNat Struct Mol Biol / PubMed:37679563 / PubMed Central
MethodsEM (single particle)
Resolution2.95 - 3.37 Å
Structure data

26165

7ty4

EMDB-26165, PDB-7ty4:
Cryo-EM structure of human Anion Exchanger 1
Method: EM (single particle) / Resolution: 2.99 Å

26167

7ty6

EMDB-26167, PDB-7ty6:
Cryo-EM structure of human Anion Exchanger 1 bound to 4,4'-Diisothiocyanatodihydrostilbene-2,2'-Disulfonic Acid (H2DIDS)
Method: EM (single particle) / Resolution: 2.98 Å

26168

7ty7

EMDB-26168, PDB-7ty7:
Cryo-EM structure of human Anion Exchanger 1 bound to Bicarbonate
Method: EM (single particle) / Resolution: 3.37 Å

26169

7ty8

EMDB-26169, PDB-7ty8:
Cryo-EM structure of human Anion Exchanger 1 bound to Niflumic Acid
Method: EM (single particle) / Resolution: 3.18 Å

26171

7tya

EMDB-26171, PDB-7tya:
Cryo-EM structure of human Anion Exchanger 1 modified with Diethyl Pyrocarbonate (DEPC)
Method: EM (single particle) / Resolution: 3.07 Å

41081

8t6u

EMDB-41081, PDB-8t6u:
Cryo-EM structure of human Anion Exchanger 1 bound to Dipyridamole
Method: EM (single particle) / Resolution: 3.13 Å

41082

8t6v

EMDB-41082, PDB-8t6v:
Cryo-EM structure of human Anion Exchanger 1 bound to 4,4'-Diisothiocyanatostilbene-2,2'-Disulfonic Acid (DIDS)
Method: EM (single particle) / Resolution: 2.95 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-HOH:
WATER

ChemComp-4DS:
4,4'-Diisothiocyano-2,2'-stilbenedisulfonic acid / inhibitor*YM

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-NFL:
2-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}NICOTINIC ACID / inhibitor*YM

ChemComp-H9F:
2-[[2-[bis(2-hydroxyethyl)amino]-4,8-di(piperidin-1-yl)pyrimido[5,4-d]pyrimidin-6-yl]-(2-hydroxyethyl)amino]ethanol / medication, inhibitor*YM

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Transmembrane

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