Brockerhoff H
FEBS Lett. 1986 May 26;201(1):1-4. doi: 10.1016/0014-5793(86)80559-2.
Membrane-bound proteins owe their retention and conformation in the lipid bilayer to hydrophobic peptide domains. Additional fixation, by protein-lipid hydrogen bonding, has been suggested, and recent reports on protein kinase C activation by diacylglycerol (DG) provide an unambiguous model for such bonding. The sn-1,2-diacylglycerol appears to donate a hydrogen bond from the sn-3 hydroxyl to the enzyme and to receive two hydrogen bonds, in the sn-1 and sn-2 ester CO groups, from the enzyme. This arrangement is confirmed in phorbol ester, a competitive inhibitor of DG for the kinase. This tumor promotor has a nearly identical spatial arrangement of hydrogen bond donor (9 alpha-OH) and acceptors (12 and 13 ester CO); so have two other tumor promotors, teleocidin and aplysiatoxin. There are reasons to believe that protein kinase C is not the only protein that is bound to membrane lipids by hydrogen bonding, and such bonding will have to be considered in membrane-associated events such as fusion, cross-membrane transport, or anesthesia.
膜结合蛋白在脂质双层中的保留和构象归因于疏水肽结构域。有人提出通过蛋白质 - 脂质氢键进行额外固定，最近关于二酰基甘油（DG）激活蛋白激酶C的报道为此类键合提供了明确的模型。sn - 1,2 - 二酰基甘油似乎从sn - 3羟基向酶提供一个氢键，并从酶在sn - 1和sn - 2酯羰基处接受两个氢键。这种排列在佛波酯中得到证实，佛波酯是DG对激酶的竞争性抑制剂。这种肿瘤促进剂具有几乎相同的氢键供体（9α - OH）和受体（12和13酯羰基）的空间排列；另外两种肿瘤促进剂，远藤霉素和海兔毒素也是如此。有理由相信蛋白激酶C不是唯一通过氢键与膜脂质结合的蛋白质，并且在诸如融合、跨膜运输或麻醉等膜相关事件中必须考虑这种键合。
