Abstract
Membrane Protein Structural Biology Minireview Series
Highlights
It is estimated that one-third of all proteins are integral membrane proteins, defined narrowly as proteins that completely traverse the membrane bilayer
There are acylated and/or prenylated proteins such as endothelial cell nitric oxide synthase (2) that depend on lipid modifications for their binding to membranes or membrane subdomains including lipid rafts (3) as well as proteins such as protein kinase C, cytosolic, Ca2ϩ-dependent phospholipase A2 (4), and protein kinase B that undergo dissociable interactions with membranes via C1 and/or C2 or pleckstrin homology or FYVE domains in the context of cellular signaling
There appear to be two major classes of integral membrane proteins, the ␣-helical transmembrane proteins broadly distributed in cellular and organellar membranes and the -barrel-containing porins found in the outer membranes of Gram-negative bacteria and mitochondrial and chloroplast membranes
Summary
It is estimated that one-third of all proteins are integral membrane proteins, defined narrowly as proteins that completely traverse the membrane bilayer. There exists a smaller but unknown number of monotopic membrane proteins, including prostaglandin endoperoxide H synthases, that interdigitate into a single leaflet of the lipid bilayer via a specific membrane binding domain (1). This four-part minireview series focuses primarily on the ␣-helical and -barrel proteins and intracellular proteins that can associate reversibly with membranes via C1 and C2 domains.
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