High-resolution structures and dynamics of membrane protein--lipid complexes: a critique.
Crystallographic analysis of lipidic components in complex with membrane proteins reveals molecules exhibiting well-ordered polar or hydrophobic moieties in contact with protein. As dynamic methods indicate high exchange rates, the interpretation of structural data requires a detailed knowledge of the specificity, affinity and cooperativity of lipid binding.
Pebay-Peyroula
E
E
IBS, UMR 5075 CEA-CNRS-UJF, F-38027 Grenoble Cedex 1, France. pebay@ibs.fr
Rosenbusch
J P
JP
D001665:Binding Sites; D002384:Catalysis; D007700:Kinetics; D008051:Lipid Bilayers / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008563:Membrane Lipids / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D011487:Protein Conformation; D014961:X-Ray Diffraction
D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins