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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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Lipid Bilayer Membrane Perturbation by Embedded Nanopores: A Simulation Study
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Bolean, M., Borin, I. A., Simão, A. M., Bottini, M., Bagatolli, L. A., Hoylaerts, M., Millán, J. L., & Ciancaglini, P. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.05.010 · Cited by 46
“A similar cluster of negatively charged lipids, a “lipid annulus”, would be expected to also surround the regions with high fluidity, however the sensitivity of our instrument was not sufficient to resolve this region [71, 72].”
Dlouhý, O., Kurasová, I., Karlický, V., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-68854-x · Cited by 46
Ramakrishnan, M., Qu, J., Pocanschi, C. L., Kleinschmidt, J. H., & Marsh, D. (2005) · Biochemistry · doi:10.1021/bi047603y · Cited by 46
“This agrees well with recent estimates for a range of ‚-barrel proteins from the E. coli outer membrane ( 50 ).”
BackgroundResultInfluentialPressure effects on lipids and bio-membrane assemblies
Brooks, N. J. (2014) · IUCrJ · doi:10.1107/s2052252514019551 · Cited by 45
“Lipid–protein interactions have increasingly been recognized as being critical to a range of cellular processes and signalling events, and it is now recognized that lipids and membrane proteins must interact strongly both physically and chemically (Lee, 2003; Charalambous et al., 2012).”
BackgroundFunctional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization
Stangl, M., & Schneider, D. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.03.011 · Cited by 45
Sinner, E., Reuning, U., Kök, F. N., et al. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.05.022 · Cited by 45
“In this context, the fact that the supramolecular structure and, thus, the binding properties of a membrane protein are crucially determined by its insertion into a lipid membrane [13] has to be taken into account .”
BackgroundGustot, A., Smriti, S., Ruysschaert, J., Mchaourab, H. S., & Govaerts, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.079673 · Cited by 46
Velikova, V., Müller, C., Ghirardo, A., et al. (2015) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.00612 · Cited by 44
Unraveling the role of the Target of Rapamycin signaling in sphingolipid metabolism
Teixeira, V., & Costa, V. (2015) · Progress in Lipid Research · doi:10.1016/j.plipres.2015.11.001 · Cited by 46
Mechanosensory Transduction: Focus on Ion Channels ☆
Martinac, B., & Cox, C. D. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.08094-8 · Cited by 48
Influence of Transmembrane Helix Mutations on Cytochrome P450-Membrane Interactions and Function
Mustafa, G., Nandekar, P. P., Camp, T., Bruce, N. J., Gregory, M. C., Sligar, S. G., & Wade, R. C. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2018.12.014 · Cited by 45
“Tryptophan (W) and Tyrosine (Y) residues in membrane proteins act as anchoring residues and are generally located between the polar headgroup and hydrophobic core of the lipid bilayer in the glycerol region of the lipid bilayer (14).”
BackgroundChattopadhyay, A., Jafurulla, M., Kalipatnapu, S., Pucadyil, T. J., & Harikumar, K. G. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.102 · Cited by 44
Expediting topology data gathering for the TOPDB database
Dobson, L., Langó, T., Reményi, I., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1119 · Cited by 43
Quantification of Protein-Lipid Selectivity using FRET: Application to the M13 Major Coat Protein
Fernandes, F., Loura, L. M. S., Koehorst, R. B. M., et al. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.040337 · Cited by 43
“Overall the selectivity of annular lipid-M13 coat protein is not large, which is common for intrinsic membrane proteins (Lee, 2003).”
BackgroundResult“Frozen” Block Copolymer Nanomembranes with Light-Driven Proton Pumping Performance
Kuang, L., Fernandes, D. A., O’Halloran, M., et al. (2013) · ACS Nano · doi:10.1021/nn4059852 · Cited by 43
Modification of membrane lipid compositions in single-celled organisms – From basics to applications
Pichler, H., & Emmerstorfer‐Augustin, A. (2018) · Methods · doi:10.1016/j.ymeth.2018.06.009 · Cited by 44
Rizzuti, B. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140757 · Cited by 43
Tuning cell surface charge in E. coli with conjugated oligoelectrolytes
Catania, C., Thomas, A. W., & Bazan, G. C. (2015) · Chemical Science · doi:10.1039/c5sc03046c · Cited by 43
Positioning Membrane Proteins by Novel Protein Engineering and Biophysical Approaches
Tatulian, S. A., Qin, S., Pande, A. H., & He, X. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.06.080 · Cited by 43
Quantification of protein–lipid selectivity using FRET
Loura, L. M. S., PRIETO, M. J. E., & Fernandes, F. (2009) · European Biophysics Journal · doi:10.1007/s00249-009-0532-z · Cited by 42
Pearlstein, R. A., Dickson, C. J., & Horn̆ák, V. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.11.005 · Cited by 42
Current Methods for Detecting Cell Membrane Transient Interactions
Bagheri, Y., Ali, A. A., & You, M. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.603259 · Cited by 41
“These membrane components dynamically interact with each other to regulate cell cycles and communications (Lee, 2003; Contreras et al., 2011; Varshney et al., 2016; Sezgin et al., 2017).”
BackgroundMembrane protein dynamics and detergent interactions within a crystal: A simulation study of OmpA
Bond, P. J., Faraldo‐Gómez, J. D., Deol, S. S., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600398103 · Cited by 42
Kangur, L., Timpmann, K., & Freiberg, A. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp801943w · Cited by 42
Self-Association of Models of Transmembrane Domains of ErbB Receptors in a Lipid Bilayer
Prakash, A., Janosi, L., & Doxastakis, M. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.10.023 · Cited by 42
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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