Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution
Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution
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DOI：
10.1126/science.276.5320.1861
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发表时间：
1997-06-20
期刊：
影响因子：
56.9
通讯作者：
Eisenberg, D
中科院分区：
文献类型：
--
作者：
Beamer, LJ;Carroll, SF;Eisenberg, D
杀菌/通透性增加蛋白(BPI)是一种由456个残基组成的有效抗菌蛋白，它结合并中和革兰氏阴性细菌外膜上的脂多糖。在2.4埃的分辨率下，人BPI的晶体结构显示由两个相似的结构域组成的回旋镖形状的分子。回旋镖凹面上的两个无极口袋，每个都结合了一个磷脂酰胆碱分子，主要是通过与它们的酰基链相互作用；这表明这些口袋也可能结合了脂多糖的酰基链。作为相关血浆脂转移蛋白的模型，BPI阐明了该蛋白家族的脂转移机制。
Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal structure of human BPI shows a boomerang-shaped molecule formed by two similar domains. Two apolar pockets on the concave surface of the boomerang each bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. As a model for the related plasma lipid transfer proteins, BPI illuminates a mechanism of lipid transfer for this protein family.