Structure and metal binding studies of the second copper binding domain of the Menkes ATPase

2003 ◽  
Vol 143 (3) ◽  
pp. 209-218 ◽  
Author(s):  
Christopher E. Jones ◽  
Norelle L. Daly ◽  
Paul A. Cobine ◽  
David J. Craik ◽  
Charles T. Dameron
Keyword(s):  
Metal Binding ◽  
Binding Domain ◽  
Copper Binding ◽  
Binding Studies ◽  
Menkes Atpase

Expression, purification and copper-binding studies of the first metal-binding domain of Menkes protein

1999 ◽  
Vol 264 (3) ◽  
pp. 890-896 ◽  
Author(s):  
Pia Y. Jensen ◽  
Nicklas Bonander ◽  
Nina Horn ◽  
Zeynep Tumer ◽  
Ole Farver
Keyword(s):  
Metal Binding ◽  
Binding Domain ◽  
Copper Binding ◽  
Binding Studies ◽  
Metal Binding Domain ◽  
Menkes Protein

Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification

2013 ◽  
Vol 454 (1) ◽  
pp. 147-156 ◽  
Author(s):  
Nataliya V. Dolgova ◽  
Sergiy Nokhrin ◽  
Corey H. Yu ◽  
Graham N. George ◽  
Oleg Y. Dmitriev
Keyword(s):  
Metal Binding ◽  
Wilson’S Disease ◽  
Wilson's Disease ◽  
Binding Domain ◽  
Binding Motif ◽  
Copper Chaperone ◽  
Copper Binding ◽  
Copper Transporters ◽  
Metal Binding Domain ◽  
Disease Protein

Human copper transporters ATP7B (Wilson's disease protein) and ATP7A (Menkes' disease protein) have been implicated in tumour resistance to cisplatin, a widely used anticancer drug. Cisplatin binds to the copper-binding sites in the N-terminal domain of ATP7B, and this binding may be an essential step of cisplatin detoxification involving copper ATPases. In the present study, we demonstrate that cisplatin and a related platinum drug carboplatin produce the same adduct following reaction with MBD2 [metal-binding domain (repeat) 2], where platinum is bound to the side chains of the cysteine residues in the CxxC copper-binding motif. This suggests the same mechanism for detoxification of both drugs by ATP7B. Platinum can also be transferred to MBD2 from copper chaperone Atox1, which was shown previously to bind cisplatin. Binding of the free cisplatin and reaction with the cisplatin-loaded Atox1 produce the same protein-bound platinum intermediate. Transfer of platinum along the copper-transport pathways in the cell may serve as a mechanism of drug delivery to its target in the cell nucleus, and explain tumour-cell resistance to cisplatin associated with the overexpression of copper transporters ATP7B and ATP7A.

scholarly journals The soluble metal-binding domain of the copper transporter ATP7B binds and detoxifies cisplatin

2009 ◽  
Vol 419 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Nataliya V. Dolgova ◽  
Doug Olson ◽  
Svetlana Lutsenko ◽  
Oleg Y. Dmitriev
Keyword(s):  
Metal Binding ◽  
Binding Sites ◽  
Active Drug ◽  
Binding Domain ◽  
Copper Binding ◽  
Protein Fragment ◽  
Copper Transporter ◽  
Metal Binding Domain ◽  
Cell Expression

Wilson disease ATPase (ATP7B) has been implicated in the resistance of cancer cells to cisplatin. Using a simple in vivo assay in bacterial culture, in the present study we demonstrate that ATP7B can confer resistance to cisplatin by sequestering the drug in its N-terminal metal-binding domain without active drug extrusion from the cell. Expression of a protein fragment containing four N-terminal MBRs (metal-binding repeats) of ATP7B (MBR1–4) protects cells from the toxic effects of cisplatin. One MBR1–4 molecule binds up to three cisplatin molecules at the copper-binding sites in the MBRs. The findings of the present study suggest that suppressing enzymatic activity of ATP7B may not be an effective way of combating cisplatin resistance. Rather, the efforts should be directed at preventing cisplatin binding to the protein.

In silico modeling of the Menkes copper-translocating P-type ATPase 3rd metal binding domain predicts that phosphorylation regulates copper-binding

BioMetals ◽  
2011 ◽  
Vol 24 (3) ◽  
pp. 477-487 ◽  
Author(s):  
N. A. Veldhuis ◽  
M. J. Kuiper ◽  
R. C. J. Dobson ◽  
R. B. Pearson ◽  
J. Camakaris
Keyword(s):  
Metal Binding ◽  
In Silico ◽  
Binding Domain ◽  
Copper Binding ◽  
Metal Binding Domain ◽  
In Silico Modeling ◽  
P Type

scholarly journals A Coiled-Coil Domain of Melanophilin Is Essential for Myosin Va Recruitment and Melanosome Transport in Melanocytes

2006 ◽  
Vol 17 (11) ◽  
pp. 4720-4735 ◽  
Author(s):  
Alistair N. Hume ◽  
Abul K. Tarafder ◽  
José S. Ramalho ◽  
Elena V. Sviderskaya ◽  
Miguel C. Seabra
Keyword(s):  
Coiled Coil ◽  
Binding Domain ◽  
Actin Binding ◽  
Binding Studies ◽  
Null Cell ◽  
Coiled Coil Region ◽  
Actin Binding Domain ◽  
Transport Assay ◽  
Myosin Va

Melanophilin (Mlph) regulates retention of melanosomes at the peripheral actin cytoskeleton of melanocytes, a process essential for normal mammalian pigmentation. Mlph is proposed to be a modular protein binding the melanosome-associated protein Rab27a, Myosin Va (MyoVa), actin, and microtubule end-binding protein (EB1), via distinct N-terminal Rab27a-binding domain (R27BD), medial MyoVa-binding domain (MBD), and C-terminal actin-binding domain (ABD), respectively. We developed a novel melanosome transport assay using a Mlph-null cell line to study formation of the active Rab27a:Mlph:MyoVa complex. Recruitment of MyoVa to melanosomes correlated with rescue of melanosome transport and required intact R27BD together with MBD exon F–binding region (EFBD) and unexpectedly a potential coiled-coil forming sequence within ABD. In vitro binding studies indicate that the coiled-coil region enhances binding of MyoVa by Mlph MBD. Other regions of Mlph reported to interact with MyoVa globular tail, actin, or EB1 are not essential for melanosome transport rescue. The strict correlation between melanosomal MyoVa recruitment and rescue of melanosome distribution suggests that stable interaction with Mlph and MyoVa activation are nondissociable events. Our results highlight the importance of the coiled-coil region together with R27BD and EFBD regions of Mlph in the formation of the active melanosomal Rab27a-Mlph-MyoVa complex.

Chemical Modification and Metal Binding Studies ofDatura innoxia

1996 ◽  
Vol 30 (1) ◽  
pp. 110-114 ◽  
Author(s):  
Lawrence R. Drake ◽  
Shan Lin ◽  
Gary D. Rayson ◽  
Paul J. Jackson
Keyword(s):  
Chemical Modification ◽  
Metal Binding ◽  
Binding Studies

scholarly journals The YcnI protein from Bacillus subtilis contains a copper-binding domain

2021 ◽  
pp. 101078
Author(s):  
Madhura S. Damle ◽  
Aarshi N. Singh ◽  
Stephen C. Peters ◽  
Veronika A. Szalai ◽  
Oriana S. Fisher
Keyword(s):  
Bacillus Subtilis ◽  
Binding Domain ◽  
Copper Binding

Copper and Zinc Promote Interactions between Membrane-Anchored Peptides of the Metal Binding Domain of the Prion Protein†

Biochemistry ◽  
2007 ◽  
Vol 46 (14) ◽  
pp. 4261-4271 ◽  
Author(s):  
Angela G. Kenward ◽  
Libero J. Bartolotti ◽  
Colin S. Burns
Keyword(s):  
Prion Protein ◽  
Metal Binding ◽  
Binding Domain ◽  
Copper And Zinc ◽  
Metal Binding Domain
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