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|Title:||Effects of magnesium ions on recombinant human furin: selective activation of hydrolytic activity upon substrates derived from virus envelope glycoprotein|
|Authors:||Izidoro, Mario A. [UNIFESP]|
Assis, Diego M. [UNIFESP]
Oliveira, Vitor [UNIFESP]
Santos, Jorge A. N. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Juliano, Luiz [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
|Publisher:||Walter de Gruyter & Co|
|Citation:||Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 391, n. 9, p. 1105-1112, 2010.|
|Abstract:||Here we report a detailed analysis of magnesium (Mg(2+)) ion effects on furin hydrolysis of fluorescent resonance energy transfer decapeptide substrates derived from canonical R-X-K/R-R furin cleavage motifs within certain viral envelope glycoproteins and eukaryotic proproteins. Using virus-derived sequences a selective activation of furin by Mg(2+) ions was observed as a result of cooperativity between furin subsites. Furin hydrolysis of the peptides Abz-SRRHKR down arrow FAGV-Q-EDDnp (from measles virus fusion protein F(o)) and Abz-RERRRKKR down arrow GLFG-Q-EDDnp (from Asian avian influenza A, H5N1) was activated between 60- and 80-fold by MgCl(2). It appears that virus envelope glycoprotein mutations have been selected to increase their susceptibility to furin within cells, a location where Mg(2+) is present in adequate concentrations for activation. Both the pH profile of furin and its intrinsic fluorescence were modified by Mg(2+) ions, which bind to furin with a K(d) value of 1.1 mM.|
|Appears in Collections:||Em verificação - Geral|
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