Projection Structure of P-glycoprotein by Electron Microscopy
Projection Structure of P-glycoprotein by Electron Microscopy
复制标题
P-糖蛋白的电子显微镜投影结构
DOI：
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发表时间：
2002
影响因子：
4.8
通讯作者：
S. Wilkens
中科院分区：
文献类型：
--
作者：
Jyh;I. Urbatsch;A. E. Senior;S. Wilkens
用电镜和图像分析方法研究了小鼠p -糖蛋白（Pgp）的结构。通过脂质单层技术重组含有c端6组氨酸标签的纯洗涤剂溶解蛋白，生成了脂质双层中的Pgp二维晶体。晶体属于P1平面群，a = b = 104±2 Å， γ = 90±4°。Pgp的投影结构以22 Å的分辨率计算，显示了两个密切相互作用的蛋白质结构域，可以解释为蛋白质的N端和c端一半。Pgp的投影结构与最近发表的MsbA的x射线结构一致，MsbA是一种来自大肠杆菌的脂质a翻转酶，与Pgp具有高度的序列同源性，但只有当两个MsbA亚基旋转以将其核苷酸结合域聚集在一起时才会发生。
The structure of P-glycoprotein (Pgp) from mouse has been studied by electron microscopy and image analysis. Two-dimensional crystals of Pgp in a lipid bilayer were generated by reconstituting pure, detergent-solubilized protein containing a C-terminal six-histidine tag using the lipid monolayer technique. The crystals belong to plane group P1 with a = b = 104 ± 2 Å and γ = 90 ± 4°. The projection structure of Pgp calculated at a resolution of 22 Å shows two closely interacting protein domains that can be interpreted as the N- and C-terminal halves of the protein. The projection structure of Pgp is consistent with the recently published x-ray structure of MsbA, a lipid A flippase from Escherichia coli with high sequence homology to Pgp but only when the two MsbA subunits are rotated to bring their nucleotide binding domains together.
巴斯德毕赤酵母细胞中表达的 N-糖基化突变小鼠和人 P-糖蛋白的纯化和表征。
影响因子：
3.9
作者：
Urbatsch,IL;Wilke-Mounts,S;Gimi,K;Senior,AE
通讯作者：
Senior,AE
影响因子：
2.9
作者：
Senior, AE;Bhagat, S
通讯作者：
Bhagat, S