Many membrane proteins selectively bind defined lipid species. This specificity has an impact on correct insertion, folding, structural integrity and full functionality of the protein. How are these different tasks achieved? Recent advances in structural research of membrane proteins provide new information about specific protein–lipid interactions. Tightly bound lipids in membrane protein structures are described and general principles of the binding interactions are deduced. Lipid binding is stabilized by multiple non-covalent interactions from protein residues to lipid head groups and hydrophobic tails. Distinct lipid-binding motifs have been identified for lipids with defined head groups in membrane protein structures. The stabilizing interactions differ between the electropositive and electronegative membrane sides. The importance of lipid binding for vertical positioning and tight integration of proteins in the membrane, for assembly and stabilization of oligomeric and multisubunit complexes, for supercomplexes, as well as for functional roles are pointed out.
Skip Nav Destination
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Conference Article| October 26 2005
Specific protein–lipid interactions in membrane proteins
C. Hunte 1
1Department of Molecular Membrane Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, D-60438 Frankfurt, Germany
Search for other works by this author on:
Biochem Soc Trans (2005) 33 (5): 938–942.
July 11 2005
C. Hunte; Specific protein–lipid interactions in membrane proteins. Biochem Soc Trans 26 October 2005; 33 (5): 938–942. doi: https://doi.org/10.1042/BST0330938
Download citation file:
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Sign in via your InstitutionSign in via your Institution
Get Access To This Article
Buy This Article