A place for thioether chemistry in cellular copper ion recognition and trafficking.
Over the last decade, cysteine thiolate ligands have been shown to be critical to the Cu(I) (cuprous) binding chemistry of many cytosolic metallochaperone and metalloregulatory proteins involved in copper physiology. More recently, the thioether group of methionine has begun to emerge as an important Cu(I) ligand for trafficking proteins in more oxidizing cellular environments.
Davis
Anna V
AV
Department of Chemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.
O'Halloran
Thomas V
TV
D000818:Animals; D001665:Binding Sites; D001692:Biological Transport; D002451:Cell Compartmentation; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D003600:Cytosol / Q000737:chemistry / Q000378:metabolism; D005057:Eukaryotic Cells / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D008715:Methionine / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D013440:Sulfides / Q000737:chemistry* / Q000378:metabolism
D008024:Ligands; D008667:Metalloproteins; D013440:Sulfides; D003300:Copper; D008715:Methionine; D003545:Cysteine