The carboxyl side chain of glutamate 681 interacts with a chloride binding modifier site that allosterically modulates the dimeric conformational state of band 3 (AE1). Implications for the mechanism of anion/proton cotransport. [electronic resource]
Producer: 20030502Description: 1589-602 p. digitalISSN:- 0006-2960
- 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid -- pharmacology
- 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid -- analogs & derivatives
- Allosteric Regulation -- drug effects
- Allosteric Site -- drug effects
- Anion Exchange Protein 1, Erythrocyte -- chemistry
- Borohydrides -- pharmacology
- Chlorides -- chemistry
- Dimerization
- Erythrocyte Membrane -- chemistry
- Glutamic Acid -- chemistry
- Humans
- Indicators and Reagents
- Ion Transport -- drug effects
- Isoxazoles -- pharmacology
- Kinetics
- Models, Chemical
- Peptide Fragments -- chemistry
- Protein Binding -- drug effects
- Protein Conformation -- drug effects
- Protein Subunits -- chemistry
- Protons
- Spectrometry, Fluorescence
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Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
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