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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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Membrane rafting: From apical sorting to phase segregation
Coskun, Ü., & Simons, K. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.043 · Cited by 72
“An increasing number of X-ray structures show that specific lipids are selected as integral components of the quaternary structure of many membrane protein complexes [100–105].”
BackgroundInteractions between Phosphatidylethanolamine Headgroup and LmrP, a Multidrug Transporter
Hakizimana, P., Masureel, M., Gbaguidi, B., Ruysschaert, J., & Govaerts, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708427200 · Cited by 72
Anionic Phospholipid Interactions with the Potassium Channel KcsA: Simulation Studies
Deol, S. S., Domene, C., Bond, P. J., & Sansom, M. S. P. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.071407 · Cited by 74
“For example, Lee distinguishes between annular and nonannular sites (7), whereas Palsdottir and Hunte define three classes of bound lipid: annular, nonannular, and integral.”
BackgroundMolecular modeling of the human multidrug resistance protein 1 (MRP1/ABCC1)
DeGorter, M. K., Conseil, G., Deeley, R. G., Campbell, R. L., & Cole, S. P. C. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.141 · Cited by 70
Rostovtseva, T. K., Gurnev, P. A., Chen, M.-Y., & Bezrukov, S. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.378778 · Cited by 70
miR-32 and its target SLC45A3 regulate the lipid metabolism of oligodendrocytes and myelin
Shin, D., Howng, S. Y. B., Ptáček, L. J., & Fu, Y. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.03.054 · Cited by 70
“The specific myelin lipid composition likely to be important for the appropriate packing of the myelin membrane and changes in lipid composition can affect lipid–protein interactions causing an altered packing of proteins in the membrane (Coetzee et al., 1996; Lee, 2003).”
Structural adaptations of proteins to different biological membranes
Pogozheva, I. D., Tristram‐Nagle, S., Mosberg, H. I., & Lomize, A. L. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.06.023 · Cited by 70
“…matter © 2013 Elsevier B.V. Al http://dx.doi.org/10.1016/j.bbamem.2013.06.023 a b s t r a c t a r t i c l e i n f o Article history: Received 29 March 2013 Received in revised form 4 June 2013 Accepted 19 June 2013 Available online 27 June 2013 Keywords: Lipid bilayer Membrane protein…”
BackgroundInfluentialThe role of lipids in membrane insertion and translocation of bacterial proteins
van Dalen, A., & KRUIJFF, B. D. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.03.007 · Cited by 73
“[130]).”
In Situ Structural Studies of Anabaena Sensory Rhodopsin in the E. coli Membrane
Ward, M. E., Wang, S., Munro, R. A., et al. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.02.018 · Cited by 69
Sphingomyelin-enriched microdomains define the efficiency of native Ca2+-triggered membrane fusion
Rogasevskaia, T. P., & Coorssen, J. R. (2006) · Journal of Cell Science · doi:10.1242/jcs.03007 · Cited by 69
“…curvature effects on membranes, contributing to the formation of transient, high-curvature membrane intermediates associated with bilayer merger (Ruiz-Argüello et al., 1996; Cremesti et al., 2002; Montes et al., 2002; Saez-Cirion et al., 2002; Van Blitterswijk et al., 2003; Contreras et al., 2005).”
BackgroundInfluentialCorey, R. A., Pyle, E., Allen, W. J., Watkins, D. W., Casiraghi, M., Miroux, B., Aréchaga, I., Politis, A., & Collinson, I. R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721536115 · Cited by 70
Cohen, E., Goldshleger, R., Shainskaya, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414290200 · Cited by 68
Mesoscale organization of domains in the plasma membrane – beyond the lipid raft
Lu, S. M., & Fairn, G. D. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1436515 · Cited by 64
Kynde, S., Skar‐Gislinge, N., Pedersen, M. C., Midtgaard, S. R., Simonsen, J. B., Schweins, R., Mortensen, K., & Arleth, L. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004713028344 · Cited by 67
“…4.73 Radius of protruding His tags (Å) — 5.8 12.5 20.4 Deduced parameters Interface area per lipid (Å2) 77.3 62.9 Bilayer thickness at rim (Å) 39.4 40.8 Bilayer thickness at centre (Å) 40.2 40.8 Bilayer circumference (Å) 272 234 would estimate the hydrophobic height to be 35 Å (Lee, 2003).”
BackgroundInfluentialThe role of lipid composition for insertion and stabilization of amino acids in membranes
Johansson, A., & Lindahl, E. R. (2009) · The Journal of Chemical Physics · doi:10.1063/1.3129863 · Cited by 67
Membrane Organization and Function of the Serotonin1A Receptor
Kalipatnapu, S., & Chattopadhyay, A. (2007) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-007-9189-2 · Cited by 67
“Lipid–protein interactions in membranes have attracted a lot of attention in relation to the role of such interactions in assembly, stability, and function of membrane proteins (Lee 2003, 2004; Palsdottir and Hunte 2004).”
BackgroundRaunser, S., & Walz, T. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133649 · Cited by 67
Importance of Direct Interactions with Lipids for the Function of the Mechanosensitive Channel MscL
Powl, A. M., East, J. M., & LEE, A. G. J. (2008) · Biochemistry · doi:10.1021/bi801352a · Cited by 66
“The activities of many integral membrane proteins have been observed to change with changes in the composition of the surrounding lipid bilayer (1, 2).”
BackgroundSelf-citationAdaptation of the bacterial membrane to changing environments using aminoacylated phospholipids
Roy, H., Dare, K., & Ibba, M. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06563.x · Cited by 66
“Lipid composition and the presence of certain phospholipids in the membrane are known to modulate the folding and activity of certain membrane proteins (Cronan, 2003; Lee, 2003), and it is attractive to think that Ala-PG might influence porin permeability either directly or indirectly, thus modulating the uptake of nu…”
BackgroundThe lipid bilayer membrane and its protein constituents
Robertson, J. (2018) · The Journal of General Physiology · doi:10.1085/jgp.201812153 · Cited by 69
“Are these lipids that are found to interact with membrane proteins in structures or mass spectrometry analogous to crystallographic waters found in soluble proteins? Or do they represent something more like ligand binding in the context of the membrane? Electron spin resonance and fluorescence-quenching studies do not…”
BackgroundMach, T., Neves, P., Spiga, E., Weingart, H., Winterhalter, M., Ruggerone, P., Ceccarelli, M., & Gameiro, P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803188c · Cited by 65
Differential Stiffness and Lipid Mobility in the Leaflets of Purple Membranes
Voı̈tchovsky, K., Contera, S., Kamihira, M., et al. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.072405 · Cited by 65
“The important role of proteinlipid interactions in the assembly and activity of PM has been widely studied, mainly by diffraction spectroscopic techniques (8,11,12).”
BackgroundCholesterol interaction motifs in G protein‐coupled receptors: Slippery hot spots?
Sarkar, P., & Chattopadhyay, A. (2020) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1481 · Cited by 65
“…with membrane proteins (and therefore remain preserved even in the crystal structure) are often localized in protein–protein interfaces in oligomeric proteins and belong to the class of “nonannular” (or sometimes termed as “co-factor”) lipids (Lee, 2003, 2005; Paila, Tiwari, & Chattopadhyay, 2009).”
BackgroundWiking, L., Gregersen, S. B., Hansen, S. F., et al. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105213 · Cited by 64
Helical membrane protein conformations and their environment
Cross, T. A., Murray, D. T., & Watts, A. G. (2013) · European Biophysics Journal · doi:10.1007/s00249-013-0925-x · Cited by 64
“The influence of specific lipid–protein interactions on membrane protein function is a relatively mature field (Marsh and Watts 1982; Lee 2003; Watts 1998; Hunte and Richers 2008), but here the focus is on the influence of membrane properties on a-helical TM protein structure and conformation at…”
BackgroundSolid-state NMR spectroscopy to study protein–lipid interactions
Huster, D. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.12.002 · Cited by 67
Comparing crystal structures of Ca2+‐ ATP ase in the presence of different lipids
Drachmann, N. D., Olesen, C., MØLLER, J. V., et al. (2014) · FEBS Journal · doi:10.1111/febs.12957 · Cited by 64
Modelling of proteins in membranes
Sperotto, M. M., May, S., & Baumgaertner, A. (2006) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2006.02.024 · Cited by 64
Lu, Y., Zhang, H., Niedzwiedzki, D. M., Jiang, J. T., Blankenship, R. E., & Gross, M. L. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b01945 · Cited by 67
Powl, A. M., East, J. M., & LEE, A. G. J. (2008) · Biochemistry · doi:10.1021/bi702409t · Cited by 64
“FIGURE 2: Rates (O) and amplitudes (4) of the fluorescence response following reaction with MTSET for MscL reconstituted in vesicles of a 1:1 molar ratio of DOPG:DOPC.”
BackgroundSelf-citation
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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