Cited by 886Lipid Membrane Structure and BehaviorProtein Structure and DynamicsReceptor Mechanisms and Signaling

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Lipid–protein interactions in biological membranes: a structural perspective

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Lee, A.G·2003·Biochimica et Biophysica Acta (BBA) - Biomembranes

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Abstract

Lipid molecules bound to membrane proteins are resolved in some high-resolution structures of membrane proteins. An analysis of these structures provides a framework within which to analyse the nature of lipid-protein interactions within membranes. Membrane proteins are surrounded by a shell or annulus of lipid molecules, equivalent to the solvent layer surrounding a water-soluble protein. The lipid bilayer extends right up to the membrane protein, with a uniform thickness around the protein. The surface of a membrane protein contains many shallow grooves and protrusions to which the fatty acyl chains of the surrounding lipids conform to provide tight packing into the membrane. An individual lipid molecule will remain in the annular shell around a protein for only a short period of time. Binding to the annular shell shows relatively little structural specificity. As well as the annular lipid, there is evidence for other lipid molecules bound between the transmembrane alpha-helices of the protein; these lipids are referred to as non-annular lipids. The average thickness of the hydrophobic domain of a membrane protein is about 29 A, with a few proteins having significantly smaller or greater thicknesses than the average. Hydrophobic mismatch between a membrane protein and the surrounding lipid bilayer generally leads to only small changes in membrane thickness. Possible adaptations in the protein to minimise mismatch include tilting of the helices and rotation of side chains at the ends of the helices. Packing of transmembrane alpha-helices is dependent on the chain length of the surrounding phospholipids. The function of membrane proteins is dependent on the thickness of the surrounding lipid bilayer, sometimes on the presence of specific, usually anionic, phospholipids, and sometimes on the phase of the phospholipid.

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Authors: Lee, A. G.
Affiliations: University of Southampton (GB)
Corresponding author: Lee, A.G
Venue: Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher: Elsevier BV
Published: 2003-05
Volume: 1612
Issue: 1
Pages: 1-40
ISSN: 0005-2736 (ISSN-L)
DOI: 10.1016/s0005-2736(03)00056-7
OpenAlex: W2128882835
Cited by: 886
References: 224
Citations by year: 2026: 31 · 2025: 30 · 2024: 25 · 2023: 16 · 2022: 32 · 2021: 33 · 2020: 31 · 2019: 51 · 2018: 37 · 2017: 33 · 2016: 32 · 2015: 51 · 2014: 47 · 2013: 38 · 2012: 32
FWCI: 3.71
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3766 d)
Locations: Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
PubMed (publishedVersion)
ePrints Soton (University of Southampton) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: protein-lipid interactions, membrane proteins, lipid bilayers, transmembrane helices, hydrophobic mismatch, membrane thickness, helix tilt, anionic phospholipids, lipid phase, membrane protein structure
MeSH terms: Animals, Bacteriorhodopsins, Crystallization, Humans, Lipid Bilayers, Membrane Lipids, Membrane Proteins, Protein Structure, Secondary, Photosynthetic Reaction Center Complex Proteins, Hydrophobic and Hydrophilic Interactions

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Lipid–protein interactions in biological membranes: a structural perspective

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