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Lipid-protein interactions in biological membranes: a structural perspective

Lipid-protein interactions in biological membranes: a structural perspective
Lipid-protein interactions in biological membranes: a structural perspective
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 ?-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 Å, 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 ?-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.
annular lipid, non-annular site, hydrophobic mismatch, membrane protein structure, lipid bilayer, lipid-protein interaction, membrane structure
0304-4165
1-40
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e

Lee, A.G. (2003) Lipid-protein interactions in biological membranes: a structural perspective. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1612 (1), 1-40. (doi:10.1016/S0005-2736(03)00056-7).

Record type: Article

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 ?-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 Å, 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 ?-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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More information

Published date: 2 May 2003
Keywords: annular lipid, non-annular site, hydrophobic mismatch, membrane protein structure, lipid bilayer, lipid-protein interaction, membrane structure

Identifiers

Local EPrints ID: 56630
URI: http://eprints.soton.ac.uk/id/eprint/56630
ISSN: 0304-4165
PURE UUID: 6b7beee3-fc13-4c3d-96e4-169bca44b57b

Catalogue record

Date deposited: 07 Aug 2008
Last modified: 15 Mar 2024 11:02

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