Substrate-dependent reversal of anion transport site orientation in the human red blood cell anion-exchange protein, AE1.
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ABSTRACT: The tightly coupled, one-for-one exchange of anions mediated by the human red blood cell AE1 anion-exchange protein involves a ping-pong mechanism, in which AE1 alternates between a state with the anion-binding site facing inward toward the cytoplasm (Ei) and a state with the site facing outward toward the external medium (Eo). The conformational shift (Ei <--> Eo) is only permitted when a suitable substrate such as Cl(-) or HCO(3)(-) (B(-)) is bound. With no anions bound, or with Cl(-) bound, far more AE1 molecules are in the inward-facing than the outward-facing forms (Ei Eo, ECli EClo). We have constructed a model for CI(-)-B(-) exchange based on Cl(-)-Cl(-) and B(-)-B(-) exchange data, and have used it to predict the heteroexchange flux under extremely asymmetric conditions, with eithe
SUBMITTER: Knauf PA
PROVIDER: S-EPMC125063 | biostudies-literature | 2002 Aug
REPOSITORIES: biostudies-literature
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