Mechanistic basis for site-site interactions in inhibitor and substrate binding to band 3 (AE1): evidence distinguishing allosteric from electrostatic effects.
Mechanistic basis for site-site interactions in inhibitor and substrate binding to band 3 (AE1): evidence distinguishing allosteric from electrostatic effects.
复制标题
抑制剂和底物与带 3 (AE1) 结合的位点相互作用的机制基础:区分变构效应和静电效应的证据。
DOI:
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发表时间:
2001
期刊:
影响因子:
--
通讯作者:
J. M. Salhany
中科院分区:
文献类型:
--
作者:
J. M. Salhany
Kinetic studies suggest that stilbenedisulfonates inhibit erythrocyte anion exchange by competing with substrate anions for binding to band 3 (AE1). Such competition seems to involve site-site interactions between distinct inhibitor and substrate binding sites. The molecular basis for site-site interactions could be allosteric or electrostatic. In this paper, inhibitor binding kinetic studies are reviewed, and 35Cl(-) NMR line-broadening experiments are presented, both of which seem to rule out an electrostatic hypothesis. The results are consistent with an allosteric site-site interaction mechanism in the binding of stilbenedisulfonate and substrate anions to band 3.
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DOI:
10.1016/s0021-9258(17)42114-4
发表时间:
1994-01
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
K. Okubo;D. Kang;N. Hamasaki;M. Jennings
通讯作者:
K. Okubo;D. Kang;N. Hamasaki;M. Jennings
DOI:
--
发表时间:
1989
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Garcia,AM;Lodish,HF
通讯作者:
Lodish,HF
影响因子:
2.9
作者:
Batenjany,MM;Mizukami,H;Salhany,JM
通讯作者:
Salhany,JM
DOI:
--
发表时间:
1994
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
VanDort,HM;Low,PS;Cordes,KA;Schopfer,LM;Salhany,JM
通讯作者:
Salhany,JM
DOI:
10.1073/pnas.92.25.11844
发表时间:
1995
影响因子:
11.1
作者:
Salhany,JM;Schopfer,LM;Kay,MM;Gamble,DN;Lawrence,C
通讯作者:
Lawrence,C