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Lipid–protein interactions in biological membranes: a structural perspective
Open accessAbstract
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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“Fatty acyl chain length alters binding constants of several membrane proteins [169], making it tempting to speculate that VLCFAs might alter neural cell membrane structure, stability, and function [170].”
From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [169]
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“The list of proteins with activities that depend on the phase properties of the surrounding lipid includes rhodopsin, dolichylphosphomannose synthase, mycoplasma Mg2+-ATPase, mitochondrial ubiquinol-cytochrome C reductase, and H+-ATPase (21, 22).”
BackgroundCoronado, S., Herrera, J., Pino, M. G., Martı́n, S., Ballesteros, L. M., & Ce�a, P. (2024) · Nanomaterials · doi:10.3390/nano14181489 · Cited by 13
Su, J., Zhao, L., Fu, R., & Tang, Z. (2025) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70329 · Cited by 11
“The proper functioning of SERCA relies on the fluidity of liquid crystalline bilayers, with higher activity observed in 18:1 PC compared to 18:0 PC [95].”
Curvature-sensing and generation by membrane proteins: a review
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Elucidating the Structural Features of ABCA1 in its Heterogeneous Membrane Environment
Sunidhi, S., Sacher, S., Atul, A., Garg, P., & Ray, A. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.803078 · Cited by 10
Electrochemically monitoring the binding of concanavalin A and ovalbumin
Sugawara, K., Yugami, A., Kadoya, T., & Hosaka, K. (2011) · Talanta · doi:10.1016/j.talanta.2011.04.003 · Cited by 10
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Substituents modulate biphenyl penetration into lipid membranes
Rashid, A., Vakurov, A. V., Mohamadi, S., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.01.023 · Cited by 10
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Kadri, L., Ferru-Clément, R., Bâcle, A., Payet, L.-A., Cantereau, A., Hélye, R., Becq, F., Jayle, C., Vandebrouck, C., & Ferreira, T. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.06.021 · Cited by 11
Glued in lipids: Lipointoxication in cystic fibrosis
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“Considering the above, one may anticipate that perturbating the fatty acid balance within PLs cannot be without consequences on the trafficking and the structure/function of transmembrane proteins, including the CFTR channel ([52, 53]; Fig.”
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“Lipid molecules which are co-crystallized with membrane proteins are often localized in protein-protein interfaces in oligomeric proteins and have been termed as ‘nonannular ’ lipids (Lee, 2003).”
BackgroundGaseous NO2 induces various envelope alterations in Pseudomonas fluorescens MFAF76a
Chautrand, T., Depayras, S., Souak, D., Kondakova, T., Barreau, M., Kentache, T., Hardouin, J., Tahrioui, A., Thoumire, O., Konto‐Ghiorghi, Y., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-11606-w · Cited by 10
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“cases, the transmembrane helices of the integral membrane proteins consist of apolar amino acids flanked by charged amino acids at the LWI region which allow stable insertion of these TMs in the lipid bilayer (Lee 2003).”
BackgroundOrientation and conformation of lipids in crystals of transmembrane proteins
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“Lipid–protein interactions both in natural membranes and in membranes reconstituted with defined lipids and purified proteins have been investigated with a variety of spectroscopic techniques: spin-label EPR, deuterium NMR, and fluorescence (Marsh and Horváth 1998; Marsh 2008a; Seelig and Seelig 1980; Oldfield 1982; B…”
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“The role of lipid-lipid bilayer in formation of proper membrane topology of P450 protein and its catalytic activity have already been documented [49,50].”
BackgroundThe changes in erythrocyte Ca2+-ATPase activity induced by PEG-1500 and low temperatures
Zemlianskykh, N. G., & Babijchuk, L. A. (2017) · Cell and Tissue Biology · doi:10.1134/s1990519x17020109 · Cited by 10
“…an increase in the bilayer thickness upon dehydration of lipid molecules can cause a mismatch of membrane domains to the lipid matrix thickness, that leads to certain restrictions of the membrane domains’ mobility necessary to implement the Ca2+ATPase conformational transformations (Lee, 2003).”
BackgroundMembrane-protein crystals for neutron diffraction
Sørensen, T. L.-M., Hjorth-Jensen, S. J., Oksanen, E., Andersen, J. L., Olesen, C., MØLLER, J. V., & Nissen, P. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318012561 · Cited by 10
“As the function of SERCA is affected by the presence of specific phospholipids (Lee, 2003), we were anticipating that SERCA crystallization could be selective for specific lipids and hence result in the accumulation of unfavourable lipids in the crystal-growth phase, which in turn would render the…”
BackgroundLEE, A. G. J. (2005) · Nature · doi:10.1038/438569a · Cited by 10
Self-citationUlmschneider, M. B., Tieleman, D. P., & Sansom, M. S. P. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp0379650 · Cited by 10
Metadata
- 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)
- 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
- 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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