EFFECT OF DELETING THE R-DOMAIN ON CFTR-GENERATED CHLORIDE CHANNELS

被引：256

作者：

RICH, DP

GREGORY, RJ

ANDERSON, MP

MANAVALAN, P

SMITH, AE

WELSH, MJ

机构：

[1] GENZYME CORP, FRAMINGHAM, MA 01701 USA

[2] MIT, HOWARD HUGHES MED INST, DEPT PHYSIOL & BIOPHYS, CAMBRIDGE, MA 02142 USA

来源：

SCIENCE | 1991年 / 253卷 / 5016期

关键词：

D O I：

10.1126/science.1712985

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The cystic fibrosis transmembrane conductance regulator (CFTR), which forms adenosine 3',5'-monophosphate (cAMP)-regulated chloride channels, is defective in patients with cystic fibrosis. This protein contains two putative nucleotide binding domains (NBD1 and NBD2) and an R domain. CFTR in which the R domain was deleted (CFTR-DELTA-R) conducted chloride independently of the presence of cAMP. However, sites within CFTR other than those deleted also respond to cAMP, because the chloride current of CFTR-DELTA-R increased further in response to cAMP stimulation. In addition, deletion of the R domain suppressed the inactivating effect of a mutation in NBD2 (but not NBD1), a result which suggests that NBD2 interacts with the channel through the R domain.

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页码：205 / 207

页数：3

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