The occluded nucleotide conformation of p-glycoprotein.
The occluded nucleotide conformation of p-glycoprotein.
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p-糖蛋白的封闭核苷酸构象。
DOI：
10.1007/s10863-005-9498-4
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发表时间：
2005
影响因子：
3
通讯作者：
Senior,AlanE
中科院分区：
文献类型：
--
作者：
Tombline,Gregory;Senior,AlanE
本文综述了E552 A/E1197 A P-糖蛋白的研究进展。这种ATP酶缺陷突变体以药物敏感的方式以最大1/1化学计量紧密地封闭MgATP。封闭的核苷酸构象似乎代表了一个短暂的，不对称的，催化中间体。我们提出了一个催化模型，将核苷酸结合结构域（NBD）二聚化和闭塞的核苷酸构象，我们推测如何催化看到P-糖蛋白可能是协调与对称的二聚体结构的隔离NBD。
We review recent work on E552A/E1197A P-glycoprotein. This ATPase-defective mutant occludes MgATP tightly with maximal 1/1 stoichiometry in drug-sensitive fashion. The occluded nucleotide conformation appears to represent a transient, asymmetric, catalytic intermediate. We present a model for catalysis incorporating nucleotide binding domain (NBD) dimerization and the occluded nucleotide conformation, and we speculate as to how catalysis seen in P-glycoprotein might be harmonized with symmetrical dimer structures of isolated NBDs.