P-糖蛋白的封闭核苷酸构象。
The occluded nucleotide conformation of p-glycoprotein.
作者信息
Tombline Gregory, Senior Alan E
机构信息
Department of Biochemistry and Biophysics, University of Rochester Medical Center, Box 712, Rochester, New York 14642, USA.
出版信息
J Bioenerg Biomembr. 2005 Dec;37(6):497-500. doi: 10.1007/s10863-005-9498-4.
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.
我们回顾了关于E552A/E1197A P-糖蛋白的近期研究工作。这种ATP酶缺陷型突变体以药物敏感的方式紧密结合MgATP，化学计量比最大为1/1。被封闭的核苷酸构象似乎代表一种短暂的、不对称的催化中间体。我们提出了一个包含核苷酸结合结构域（NBD）二聚化和被封闭核苷酸构象的催化模型，并推测P-糖蛋白中的催化作用如何与分离的NBD的对称二聚体结构相协调。
Zotero 插件