Overexpression of mammalian integral membrane proteins for structural studies.
Recent successes in the determination of atomic resolution structures of integral membrane proteins have relied on purifying the proteins from abundant natural sources. In contrast, the majority of mammalian receptors, ion channels and transporters need to be overexpressed to obtain sufficient material for structural studies. This has often proved to be very difficult. Overexpression studies on a wide range of mammalian membrane proteins have shown that a few can be expressed functionally in bacteria, but many others require an insect or mammalian cell host for activity or high level expression. The serotonin transporter, which has been expressed in all the major hosts available, is a good example that has given insights into the problem of overexpressing mammalian membrane proteins for structural studies.
Tate
C G
CG
MRC Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK. cgt@mrc-lmb.cam.ac.uk
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry; D026901:Membrane Transport Proteins; D009419:Nerve Tissue Proteins; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D050486:Serotonin Plasma Membrane Transport Proteins
D002352:Carrier Proteins; D018076:DNA, Complementary; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D009419:Nerve Tissue Proteins; C493230:SLC6A4 protein, human; D050486:Serotonin Plasma Membrane Transport Proteins