How lipids and proteins interact in a membrane: a molecular approach
a School of Biological Sciences, University of Southampton, Southampton, SO16 7PX, UK
E-mail:agl@soton.ac.uk
Tel: 44 (0)23 8059 4331
Abstract
Membraneproteins in a biological membrane are surrounded by a shell or annulus of ‘solvent’lipid molecules. Theselipid molecules in general interact rather non-specifically with theprotein molecules, although a few ‘hot-spots’ may be present on theprotein where anioniclipids bind with high affinity. Because of the low structural specificity of most of the annular sites, the composition of thelipid annulus will be rather similar to the bulklipid composition of the membrane. The structures of thesolventlipid molecules are important in determining the conformational state of a membraneprotein, and hence its activity, through charge and hydrogen bonding interactions between the lipid headgroups and residues in theprotein, and through hydrophobic matching between theprotein and the surroundinglipid bilayer. Evidence is also accumulating for the presence of ‘co-factor’lipid molecules binding with high specificity to membraneproteins, often between transmembrane α-helices, and often being essential for activity.
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- Article type
- Review Article
- Submitted
- 31 Mar 2005
- Accepted
- 04 Jul 2005
- First published
- 14 Jul 2005
Permissions
Howlipids andproteins interact in a membrane: a molecular approach
A. G. Lee,Mol. BioSyst., 2005, 1, 203DOI: 10.1039/B504527D
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