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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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“Moreover, it has been shown for other P-type ATPases that the hydrophobic thickness of the surrounding bilayer exerts an effect over the enzyme activity (5, 15, 16).”
BackgroundDomènech, Ò., Torrent‐Burgués, J., Merino, S. T., et al. (2005) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2004.12.012 · Cited by 30
Cheng, M. H., Liu, L. T., Saladino, A. C., et al. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp075467b · Cited by 30
Pucadyil, T. J., Shrivastava, S. K., & Chattopadhyay, A. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.004 · Cited by 30
Febo‐Ayala, W., Morera-Félix, S. L., Hrycyna, C. A., et al. (2006) · Biochemistry · doi:10.1021/bi061159c · Cited by 30
“For example, some integral membrane protein enzymes such as Ca2+-ATPase do not retain their functional conformation in gel phase lipid bilayers ( 38 ).”
BackgroundHorn, J. N., Kao, T., & Grossfield, A. M. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7423-0_5 · Cited by 29
Ferreira, R. J., Ferreira, M. U., & dos Santos, D. J. V. A. (2014) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1196 · Cited by 30
Elibol, B., Jakubowska-Doğru, E., Severcan, M., & Severcan, F. (2011) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2011.01556.x · Cited by 29
“The variations in the parameters related to lipid structure and content may affect the functions of receptors and ion channels and therefore may perturb neural processes (Awayda et al., 2004; Garip and Severcan, 2010; Lee, 2003).”
BackgroundA Lipid-mediated Quality Control Process in the Golgi Apparatus in Yeast
Pineau, L., Bonifait, L., Berjeaud, J., et al. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-06-0600 · Cited by 29
“The presence of HII promoting lipids results in curvature stress, a biophysical parameter of membranes that has been reported to regulate the folding and/or activity of integral proteins (for reviews, see Lee, 2003; van den Brinkvan der Laan et al., 2004).”
BackgroundInfluence of membrane lipid composition on the structure and activity of γ-secretase
Aguayo‐Ortiz, R., Straub, J. E., & Domı́nguez, L. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp04138e · Cited by 29
Chemistry and Function of Phospholipids
Akoh, C. C., & MIN, D. B. S. (2008) · CRC Press eBooks · doi:10.1201/9781420046649-7 · Cited by 29
Proteins, chlorophylls and lipids: X-ray analysis of a three-way relationship
Fyfe, P. K., Hughes, A. V., Heathcote, P., et al. (2005) · Trends in Plant Science · doi:10.1016/j.tplants.2005.04.007 · Cited by 29
Quantification of helix–helix binding affinities in micelles and lipid bilayers
Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I. (2004) · Protein Science · doi:10.1110/ps.04850804 · Cited by 29
“…example, the GpA dimer is partially stabilized by a small entropic contribution (Fisher et al. 1999) that may originate from the gain of conformational freedom by detergent molecules that are released during association of the peptides, similar to annular lipids (Marsh and Horvath 1998; Lee 2003).”
BackgroundStangl, M., Veerappan, A., Kroeger, A., et al. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.11.004 · Cited by 28
“Hydrophobic mismatch can result in severe destabilization of TM protein structures (47,48).”
BackgroundWhere Biology Meets Physics—A Converging View on Membrane Microdomain Dynamics
Destainville, N., Schmidt, T. H., & Lang, T. (2015) · Current topics in membranes · doi:10.1016/bs.ctm.2015.10.004 · Cited by 28
Chen, J., Raeymaecker, J. D., Hovgaard, J. B., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778431 · Cited by 28
“Indeed, it was already previously proposed that the SERCA1a Tg pocket might be a CL regulation site (39, 54).”
BackgroundArtigas, P., Alaref, S. J., Hobart, E. A., et al. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.026070 · Cited by 28
“Lipid bilayers are elastic bodies (Evans and Hochmuth, 1978), and membrane proteins undergo conformational changes that involve the protein/bilayer boundary (Lee, 2003).”
BackgroundMotional Restrictions of Membrane Proteins: A Site-Directed Spin Labeling Study
Stopar, D., Štrancar, J., Spruijt, R. B., et al. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.090308 · Cited by 28
“In general, there are also only a few references to the detailed structure analysis of other membrane proteins in mismatching lipids (1).”
BackgroundRamakrishnan, M., Pocanschi, C. L., Kleinschmidt, J. H., & Marsh, D. (2004) · Biochemistry · doi:10.1021/bi048858e · Cited by 28
Influence of lipid chain unsaturation on membrane-bound melittin: a fluorescence approach
Raghuraman, H., & Chattopadhyay, A. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.008 · Cited by 28
“Membrane lipids play an important role in organizing biological membranes, mediating the formation of functional membrane domains, and modulating the structure and function of membrane proteins [42].”
BackgroundShearer, J., & Khalid, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-20227-1 · Cited by 26
van Hilten, N., Stroh, K. S., & Risselada, H. J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00250 · Cited by 27
“…(“rafts”) (Schäfer and Marrink, 2010; Nickels et al., 2015; Belička et al., 2017; Park and Im, 2018), membrane junctions [e.g., membrane fusion intermediates (Risselada et al., 2014; Tsai et al., 2014; Smirnova et al., 2019), and transmembrane proteins (Lee, 2003; Corradi et al., 2018)].”
BackgroundOrchestration of membrane receptor signaling by membrane lipids
Arish, M., Husein, A., Kashif, M., Sandhu, P., Hasnain, S. E., Akhter, Y., & Rub, A. (2015) · Biochimie · doi:10.1016/j.biochi.2015.04.005 · Cited by 27
van Duyl, B. Y., Meeldijk, H. J. D., Verkleij, A. J., et al. (2005) · Biochemistry · doi:10.1021/bi047937n · Cited by 27
“For example, hydrophobic mismatch between the length of the transmembrane segments of integral proteins and the bilayer thickness of the membrane has been shown to affect the activity of a number of different membrane proteins (for reviews, see refs 2 - 4 ).”
A combined lipidomic and proteomic profiling of Arabidopsis thaliana plasma membrane
Bahammou, D., Recorbet, G., Cassim, A. M., Robert, F., Balliau, T., Delft, P. V., Haddad, Y., Mongrand, S., Fouillen, L., & Simon-Plas, F. (2024) · The Plant Journal · doi:10.1111/tpj.16810 · Cited by 32
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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