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Sequence homologies between nucleotide binding regions of CFTR and G‐proteins suggest structural and functional similarities

机译:CFTR和G蛋白的核苷酸结合区之间的序列同源性表明结构和功能相似

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>Sequence homology between the α-subunits of G-proteins and other GTP-binding proteins and certain regions within the nucleotide binding domains (NBDs) of cystic fibrosis transmembrane conductance regulator (CFTR) indicates that these protein structures may be similar. A sequence allignment of the NBDs of CFTR and NBDs from other membrane transporters, forms the basis of a structural model. This model predicts that one of the conserved sequences GGQR, within which a number of CF mutations occur, forms part of the nucleotide binding pocket and serves as an ON/OFF conformational switch as observed in GTP binding proteins. Furthermore, based on subtle sequence differences between the first and second NBDs of CFTR and from structure-activity data, we suggest that the nucleotide binding site environments of the two NBDs are different.
机译:p蛋白和其他GTP结合蛋白的α亚基与囊性纤维化跨膜电导调节剂(CFTR)的核苷酸结合域(NBD)内的某些区域之间的序列同源性表明,这些蛋白结构可能相似。 CFTR的NBD和其他膜转运蛋白的NBD的序列分配形成了结构模型的基础。该模型预测,其中发生多个CF突变的保守序列GGQR之一,构成核苷酸结合袋的一部分,并充当GTP结合蛋白中所观察到的ON / OFF构象转换。此外,基于CFTR的第一个和第二个NBD之间的细微序列差异以及结构活性数据,我们建议两个NBD的核苷酸结合位点环境不同。

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