Identification of specific lipid-binding sites in integral membrane proteins.
Protein-lipid interactions are increasingly recognized as central to the structure and function of membrane proteins. However, with the exception of simplified models, specific protein-lipid interactions are particularly difficult to highlight experimentally. Here, we used molecular dynamics simulations to identify a specific protein-lipid interaction in lactose permease, a prototypical model for transmembrane proteins. The interactions can be correlated with the functional dependence of the protein to specific lipid species. The technique is simple and widely applicable to other membrane proteins, and a variety of lipid matrices can be used.
Structure and Function of Biological Membranes, Université Libre de Bruxelles, Boulevard du Triomphe-CP 263, B-1050 Brussels, Belgium. marc.lensink@ulb.ac.be
Marc F
MF
Lensink
Cédric
C
Govaerts
Jean-Marie
JM
Ruysschaert
D001665:Binding Sites; D006860:Hydrogen Bonding; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D010713:Phosphatidylcholines / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation
D008051:Lipid Bilayers; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D010713:Phosphatidylcholines; C021499:lactose permease