Dynamic helix interactions in transmembrane signaling.
Studying how protein transmembrane domains transmit signals across membranes is beset by unique challenges. Here, we discuss the circumstances that have led to success and reflect on what has been learned from these examples. Such efforts suggest that some of the most interesting properties of transmembrane helix interactions may be the least amenable to study by current techniques.
Matthews
Erin E
EE
Department of Chemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA.
Zoonens
Manuela
M
Engelman
Donald M
DM
D002462:Cell Membrane / Q000737:chemistry / Q000235:genetics; D008051:Lipid Bilayers / Q000737:chemistry; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008823:Micelles; D008958:Models, Molecular; D008961:Models, Structural; D009154:Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction
D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins; D008823:Micelles; D011956:Receptors, Cell Surface; D011505:Protein-Tyrosine Kinases