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 t...

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Veröffentlicht in:	Current Opinion in Structural Biology 2001-08, Vol.11 (4), p.427-432
Hauptverfasser:	Pebay-Peyroula, Eva, Rosenbusch, Jurg P
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Boundary lipids Catalysis electron diffraction glycolipids high-resolution structures of membrane proteins Kinetics Lipid Bilayers - chemistry lipid–protein association Magnetic Resonance Spectroscopy membrane dynamics membrane insertion Membrane Lipids - chemistry Membrane Lipids - metabolism Membrane Proteins - chemistry Membrane Proteins - metabolism Models, Biological neutron scattering Protein Conformation signal transmission X-ray crystallography X-Ray Diffraction
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Zusammenfassung:	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.
ISSN:	0959-440X 1879-033X
DOI:	10.1016/S0959-440X(00)00228-1