Circular dichroism, emission, and exafs studies of Ag(I), Cd(II), Cu(I), and Hg(II) binding to metallothioneins and modeling the metal binding site

1999 ◽  
pp. 23-35 ◽  
Author(s):  
Martin J. Stillman ◽  
Anna Rae Green ◽  
Ziqi Gui ◽  
David Fowle ◽  
P. Anthony Presta
Keyword(s):  
Circular Dichroism ◽  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
Circular Dichroïsm

Unraveling the Substrate−Metal Binding Site of Ferrochelatase:  An X-ray Absorption Spectroscopic Study†

Biochemistry ◽  
2002 ◽  
Vol 41 (15) ◽  
pp. 4809-4818 ◽  
Author(s):  
Gloria C. Ferreira ◽  
Ricardo Franco ◽  
Arianna Mangravita ◽  
Graham N. George
Keyword(s):  
Spectroscopic Study ◽  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
X Ray ◽  
Substrate Metal ◽  
X Ray Absorption

Construction of an additional metal-binding site in human metallothionein-2

2006 ◽  
Vol 101 (4) ◽  
pp. 354-360 ◽  
Author(s):  
Mitsutoshi Toyama ◽  
Mariko Sasaki ◽  
Noriaki Hirayama ◽  
Yoshikatsu Murooka ◽  
Mitsuo Yamashita
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site

scholarly journals Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains

2012 ◽  
Vol 23 (19) ◽  
pp. 3801-3813 ◽  
Author(s):  
Batbileg Bor ◽  
Christina L. Vizcarra ◽  
Martin L. Phillips ◽  
Margot E. Quinlan
Keyword(s):  
Circular Dichroism ◽  
Binding Site ◽  
Actin Polymerization ◽  
Intramolecular Interaction ◽  
Hydrodynamic Analysis ◽  
A Site ◽  
Circular Dichroïsm

Formins are a conserved family of proteins known to enhance actin polymerization. Most formins are regulated by an intramolecular interaction. The Drosophila formin, Cappuccino (Capu), was believed to be an exception. Capu does not contain conserved autoinhibitory domains and can be regulated by a second protein, Spire. We report here that Capu is, in fact, autoinhibited. The N-terminal half of Capu (Capu-NT) potently inhibits nucleation and binding to the barbed end of elongating filaments by the C-terminal half of Capu (Capu-CT). Hydrodynamic analysis indicates that Capu-NT is a dimer, similar to the N-termini of other formins. These data, combined with those from circular dichroism, suggest, however, that it is structurally distinct from previously described formin inhibitory domains. Finally, we find that Capu-NT binds to a site within Capu-CT that overlaps with the Spire-binding site, the Capu-tail. We propose models for the interaction between Spire and Capu in light of the fact that Capu can be regulated by autoinhibition.

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