Lipid-protein interactions and the function of the Ca2+-ATPase of sarcoplasmic reticulum.
Regardless of the nature of the protein constituents of membranes, the molecular arrangement of lipids interacting with them must satisfy hydrophobic, ionic, and steric requirements. Biological membranes have a great diversity of lipid constituents, and this diversity might have functional roles. It has been proposed, for example, that the hydrophobic regions of membrane proteins are stabilized in the membrane through interactions with lipids able to adopt configurations other than the bilayer structure. Progress in understanding at the molecular level how lipid-protein interactions control the properties of membrane proteins has been hindered by the lack of information concerning the structure of the hydrophobic regions of membrane proteins. Nevertheless, there are many examples in the literature describing how changes in the lipid environment affect physical and biochemical properties of membrane proteins. From these studies, discussed in this review, an overall picture of how lipids and proteins interact in membranes is beginning to emerge.
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000502:physiology*; D002463:Cell Membrane Permeability; D003902:Detergents; D008563:Membrane Lipids / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology*; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D012995:Solubility; D013329:Structure-Activity Relationship; D013696:Temperature
D003902:Detergents; D008563:Membrane Lipids; D008565:Membrane Proteins; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D000252:Calcium-Transporting ATPases; D002118:Calcium