Striated domains: self-organizing ordered assemblies of transmembrane alpha-helical peptides and lipids in bilayers.
This review summarizes the knowledge on striated domains, which are ordered assemblies of transmembrane peptides and lipids under gel-state conditions. The structure, mechanism of function and utility of this system as a model for domain formation is described, resulting in a molecular description of the domains and a discussion on the relevance of these insights for the function/formation and structure of similar domains in biological membranes.
de Kruijff
Ben
B
Department of Biochemistry of Membranes, Institute of Biomembranes, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, The Netherlands. b.dekruijff@chem.uu.nl
Killian
J Antoinette
JA
Ganchev
Dragomir N
DN
Rinia
Hilde A
HA
Sparr
Emma
E
D002462:Cell Membrane / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure; D018625:Microscopy, Atomic Force; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
D008051:Lipid Bilayers; D008055:Lipids; D008565:Membrane Proteins; D010455:Peptides