Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding
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Highlights
► Kinetic parameters of anion transport of C-terminal AE1 mutants were evaluated. ► Vmax decreased as the hydrophobicities of C-terminal residues increased. ► Arg 901 modification with HPG or PG increased alkali and protease resistance. ► Increase of C-terminal hydrophobicity leads to inefficient conformational change.
Abbreviations
AE1
anion exchanger 1
C12E8
octaethyleneglycol monododecyl ether
DEPC
diethylpyrocarbonate
DIDS
4,4-diisothiocyanostilbene-2,2-disulfonic acid
GPA
glycophorin A
HPG
hydroxyphenylglyoxal
PG
phenylglyoxal
PMSF
phenylmethanesulfonyl fluoride
TCA
trichloroacetic acid
TM
transmembrane spanning portion
Keywords
Band 3 protein
Anion exchange
Membrane protein structure
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Present address: T. Y.; Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Kyoto University, 46–29 Yoshida Shimoadachi-cho, Sakyo-ku, Kyoto 606–8501, Japan.
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