Human erythrocyte anion exchange site characterised using a fluorescent probe

Nature ◽  
1979 ◽  
Vol 282 (5738) ◽  
pp. 520-522 ◽  
Author(s):  
James A. Dix ◽  
A. S. Verkman ◽  
A. K. Solomon ◽  
L. C. Cantley
Keyword(s):  
Fluorescent Probe ◽  
Anion Exchange ◽  
Human Erythrocyte ◽  
Exchange Site

scholarly journals The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange

1983 ◽  
Vol 213 (3) ◽  
pp. 577-586 ◽  
Author(s):  
C J Brock ◽  
M J A Tanner ◽  
C Kempf
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mechanism ◽  
Anion Exchange ◽  
Human Erythrocyte ◽  
Exchange Process ◽  
Anion Transport ◽  
Transport Protein ◽  
British Library ◽  
Alpha Helices

The N-terminal 72 residues of an integral membrane fragment, P5, of the human erythrocyte anion-transport protein, which is known to be directly involved in the anion-exchange process, was shown to have the following amino acid sequence: Met-Val-Pro-Lys-Pro-Gln-Gly-Pro-Leu-Pro-Asn-Thr-Ala-Leu-Leu-Ser-Leu-Val-Leu-Met -Ala-Gly-Thr-Phe-Phe-Phe-Ala-Met-Met-Leu-Arg-Lys-Phe-Lys-Asn-Ser-Ser-Tyr-Phe-Pro-Gly-Lys-Leu-Arg-Arg-Val-Ile-Gly-Asp-Phe-Gly-Val-Pro-Ile-Ser-Ile-Leu-Ile-Met-Val-Leu-Val-Asp-Phe-Phe-Ile-Gln-Asp-Thr-Tyr-Thr-Gln- The structure of this fragment was analysed, with account being taken of the constraints that apply to the folding of integral membrane proteins and the topographical locations of various sites in the sequence. It was concluded that this sequence forms two transmembrane alpha-helices. These are probably part of a cluster of amphipathic transmembrane alpha-helices, which could comprise that part of the protein responsible for transport activity. The presently available evidence relating to the anion-exchange process was considered with the structural features noted in this study and a possible molecular mechanism is proposed. In this model the rearrangement of a network of intramembranous charged pairs mediates the translocation of an anion between anion-binding regions at each surface of the membrane, which are composed of clusters of positively charged amino acids. This model imposes a sequential exchange mechanism on the system. Supplementary material, including Tables and Figures describing the compositions of peptides determined by amino acid analysis and sequence studies, quantitative and qualitative data that provide a residue-by-residue justification for the sequence assignment and a description of modifications to and use of the solid-phase sequencer has been deposited as Supplementary Publication SUP 50123 (12 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained as indicated in Biochem. J. (1983) 209, 5.

Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer

Biochemistry ◽  
1979 ◽  
Vol 18 (21) ◽  
pp. 4505-4516 ◽  
Author(s):  
Anjana Rao ◽  
Paul Martin ◽  
Reinhart A. F. Reithmeier ◽  
Lewis C. Cantley
Keyword(s):  
Energy Transfer ◽  
Binding Site ◽  
Anion Exchange ◽  
Human Erythrocyte ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Exchange System
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