The protein-lipid interface:: perspectives from magnetic resonance and crystal structures

被引：57

作者：

Marsh, D ^{[1
]}

Páli, T

机构：

[1] Max Planck Inst Biophys Chem, Spekt Abt, D-37070 Gottingen, Germany

[2] Biol Res Ctr, Inst Biophys, H-6701 Szeged, Hungary

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2004年 / 1666卷 / 1-2期

关键词：

spin-label; EPR; torsion angle; order parameter; PDC-109; seminal plasma protein; acetylcholine receptor; phospholamban; avidin; cytochrome oxidase; cytochrome c; myelin proteolipid; myelin basic protein; biotinyl lipid; local anaesthetic;

D O I：

10.1016/j.bbamem.2004.08.006

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：

Lipid-protein interactions in membranes are dynamic, and consequently are well studied by magnetic resonance spectroscopy. More recently, lipids associated with integral membrane proteins have been resolved in crystals by X-ray diffraction, mostly at cryogenic temperatures. The conformation and chain ordering of lipids in crystals of integral proteins are reviewed here and are compared and contrasted with results from magnetic resonance and with the crystal structures of phospholipid bilayers. Various aspects of spin-label magnetic resonance studies on lipid interactions with single integral proteins are also reviewed: specificity for phosphatidylcholine, competition with local anaesthetics, oligomer formation of single transmembrane helices, and protein-linked lipid chains. Finally, the interactions between integral proteins and peripheral or lipid-linked proteins, as reflected by the lipid-protein interactions in double reconstitutions, are considered. (C) 2004 Elsevier B.V, All rights reserved.

引用

页码：118 / 141

页数：24

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