Novel model peptide for Atx1-like metallochaperones.
The novel cyclodecapeptide c(GMTCSGCSRP) is able to bind soft metals with a selectivity for Hg(2+) and Cu(+) over Pb(2+), Cd(2+) and Zn(2+), and is demonstrated to be an excellent structural model of the binding loop of the copper metallochaperone Atx1 in its apo and mercury loaded forms.
Sénèque
Olivier
O
Laboratoire de Reconnaissance Ionique, SCIB, CEA/DSM/DRFMC, CEA-Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France.
Crouzy
Serge
S
Boturyn
Didier
D
Dumy
Pascal
P
Ferrand
Michel
M
Delangle
Pascale
P
D001665:Binding Sites; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D027682:Cation Transport Proteins / Q000737:chemistry / Q000378:metabolism; D003300:Copper / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008667:Metalloproteins / Q000737:chemistry*; D008670:Metals / Q000737:chemistry; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
C093341:ATX1 protein, S cerevisiae; D002352:Carrier Proteins; D027682:Cation Transport Proteins; D008667:Metalloproteins; D008670:Metals; D018832:Molecular Chaperones; D009842:Oligopeptides; D029701:Saccharomyces cerevisiae Proteins; D003300:Copper