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Lipids in membrane protein structures
被引:317
|作者:
Palsdottir, H
[1
]
Hunte, C
[1
]
机构:
[1] Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60439 Frankfurt, Germany
来源:
关键词:
lipid;
membrane protein;
lipid-protein interaction;
X-ray structure;
phospholipid;
cardiolipin;
D O I:
10.1016/j.bbamem.2004.06.012
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
This review describes the recent knowledge about tightly bound lipids in membrane protein structures and deduces general principles of the binding interactions. Bound lipids are grouped in annular, nonarmular, and integral protein lipids. The importance of lipid binding for vertical positioning and tight integration of proteins in the membrane, for assembly and stabilization of oligomeric and multisubunit complexes, for supercomplexes, as well as their functional roles are pointed out. Lipid binding is stabilized by multiple noncovalent interactions from protein residues to lipid head groups and hydrophobic tails. Based on analysis of lipids with refined head groups in membrane protein structures, distinct motifs were identified for stabilizing interactions between the phosphodiester moieties and side chains of amino acid residues. Differences between binding at the electropositive and electronegative membrane side, as well as a preferential binding to the latter, are observed. A first attempt to identify lipid head group specific binding motifs is made. A newly identified cardiolipin binding site in the yeast cytochrome bc, complex is described. Assignment of unsaturated lipid chains and evolutionary aspects of lipid binding are discussed. (C) 2004 Elsevier B.V. All rights reserved.
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页码:2 / 18
页数:17
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