The implications of the structure of the bactericidal/permeability-increasing protein on the lipid-transfer function of the cholesteryl ester transfer protein
The implications of the structure of the bactericidal/permeability-increasing protein on the lipid-transfer function of the cholesteryl ester transfer protein
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DOI：
10.1016/s0959-440x(98)80118-8
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发表时间：
1998-08-01
影响因子：
6.8
通讯作者：
Tall, AR
中科院分区：
文献类型：
--
作者：
Bruce, C;Beamer, LJ;Tall, AR
胆固醇酯转移蛋白（CETP）与杀菌/通透性增加蛋白（BPI）在进化上相关。最近解决的BPI结构显示了一个细长的，回飞镖形的分子，有两个疏水口袋开口到其凹侧。这些口袋每个都含有一个磷脂分子。CETP的模型，最近解决的BPI的晶体结构的基础上，提供了解释CETP的功能研究的基础。在该模型中，C-末端残基461-476（其被证明是血浆脂蛋白之间的中性脂质转移所需的）形成覆盖N-末端口袋的开口的两亲性螺旋。CETP的一个可能的脂质转移机制，与涉及的脂质在脂蛋白表面的无序的初始步骤，然后由翻转和进入的脂质分子进入疏水性脂质结合口袋，是假设在光的结构证据和最近的研究。
The cholesteryl ester transfer protein (CETP) is evolutionarily related to the bactericidal/permeability-increasing protein (BPI). The recently solved structure of BPI shows an elongated, boomerang-shaped molecule, with two hydrophobic pockets opening to its concave side. These pockets each contain a phospholipid molecule. A model of CETP, based on the recently solved crystal structure of BPI, provides the basis for interpreting functional studies on CETP. In this model, C-terminal residues 461-476, which were shown to be required for neutral lipid transfer between plasma lipoproteins, form an amphipathic helix covering the opening of the N-terminal pocket. A possible lipid-transfer mechanism for CETP, with the initial step involving the disordering of lipids in the lipoprotein surface, followed by the flipping and entry of a lipid molecule into the hydrophobic lipid-binding pocket, is hypothesized in light of structural evidence and recent studies.