Stoichiometry of lipid interactions with transmembrane proteins--Deduced from the 3D structures.

ABSTRACT: The stoichiometry of the first shell of lipids interacting with a transmembrane protein is defined operationally by the population of spin-labeled lipid chains whose motion is restricted directly by the protein. Interaction stoichiometries have been determined experimentally for a wide range of alpha-helical integral membrane proteins by using spin-label ESR spectroscopy. Here, we determine the spatially defined number of first-shell lipids at the hydrophobic perimeter of integral membrane proteins whose 3D structure has been determined by X-ray crystallography and lipid-protein interactions characterized by spin-labeling. Molecular modeling is used to build a single shell of lipids surrounding transmembrane structures derived from the PDB. Constrained energy optimization of the protein-li

SUBMITTER: Pali T 

PROVIDER: S-EPMC2242517 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature