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Lipids in Membrane Protein Structures

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Palsdottir,  Hildur
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Hunte,  Carola
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Palsdottir, H., & Hunte, C. (2004). Lipids in Membrane Protein Structures. Biochimica et Biophysica Acta: BBA, 1666(1-2), 2-18. doi:10.1016/j.bbamem.2004.06.012.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DAD0-8
Abstract
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, nonannular, 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 bc1 complex is described. Assignment of unsaturated lipid chains and evolutionary aspects of lipid binding are discussed.