Transmembrane domains in the functions of Fc receptors.
In the present study, we use a novel method, PHDhtm, to predict the exact locations and extents of the transmembrane (TM) domains of multisubunit immunoglobulin Fc-receptors. Whereas most previous studies have used single residue hydrophobicity plots for characterizing of these domains, PHDhtm utilizes a system of neural networks and the evolutionary information contained in multiple alignments of related sequences to predict the above. Present PHDhtm application predicts TM domains of immunoglobulin Fc-receptors that in many cases differ significantly from those derived by using earlier methods. Comparisons of helical wheel projections of the presently derived TM domains from PHDhtm with those produced earlier reveal different hydrophobic moments as well as hydrophobic and hydrophilic surfaces. These differences probably alter the character of subunit association within the receptor complexes. This new algorithm can also be used for other membrane protein complexes and may advance both understanding the principles underlying such complexes formation and design of peptides that can interfere with such TM domain association so as to modulate specific cellular responses.
Zidovetzki
Raphael
R
Department of Cell Biology and Neuroscience, University of California, Riverside, CA 92521, USA. raphael.zidovetzki@ucr.edu
Rost
Burkhard
B
Armstrong
Don L
DL
Pecht
Israel
I
D000595:Amino Acid Sequence; D000818:Animals; D004285:Dogs; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008566:Membranes / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D011961:Receptors, Fc / Q000737:chemistry / Q000378:metabolism*
D008565:Membrane Proteins; D011961:Receptors, Fc