Related ArticlesAn NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
FEBS J. 2005 Feb;272(3):865-71
Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR. The study was carried out through titrations involving HAH1 and either the second or the fifth soluble domains of ATP7A (MNK2 and MNK5, respectively), in the presence of copper(I). The copper-transfer properties of MNK2 and MNK5 are similar, and differ significantly from those previously observed for the yeast homologous system. In particular, no stable adduct is formed between either of the MNK domains and HAH1. The copper(I) transfer reaction is slow on the time scale of the NMR chemical shift, and the equilibrium is significantly shifted towards the formation of copper(I)-MNK2/MNK5. The solution structures of both apo- and copper(I)-MNK5, which were not available, are also reported. The results are discussed in comparison with the data available in the literature for the interaction between HAH1 and its partners from other spectroscopic techniques.
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Fabio Arnesano, Lucia Banci, Ivano Bertini, Isabella C. Felli, Maurizio Losacco and Giovanni Natile
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207346p/aop/images/medium/ja-2011-07346p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207346p
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9nWkAzWuq20
nmrlearner
Journal club
0
10-24-2011 11:06 PM
Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net
Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net
<img alt="" height="1" width="1" />
Biochemists reveal interaction between tumor suppressor protein and chaperone
News-Medical.net
Using nuclear magnetic resonance (NMR) spectroscopy, the scientists at the Bavarian NMR Center in Garching were able for the first time to characterize the interaction surfaces between Hsp90 and p53 and show that p53 binds to Hsp90 in an already ...
Read here
nmrlearner
Online News
0
09-08-2011 08:24 AM
[NMR paper] A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
Related Articles A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains.
J Biol Chem. 2005 Nov 18;280(46):38259-63
Authors: Banci L, Bertini I, Cantini F, Chasapis CT, Hadjiliadis N, Rosato A
ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II),
Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies.
Related Articles Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies.
J Am Chem Soc. 2005 Jan 26;127(3):996-1006
Authors: Gaggelli E, Bernardi F, Molteni E, Pogni R, Valensin D, Valensin G, Remelli M, Luczkowski M, Kozlowski H
The synthetic peptide encompassing residues 106-126 (PrP106-126, KTNMKHMAGAAAAGAVVGGLG) of the human prion protein was considered for...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] An NMR and circular dichroism study of the interaction of thiocyanate with human and
An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Related Articles An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Biophys Chem. 2003 Dec 1;106(3):233-40
Authors: Sau AK, Currell D, Mazumdar S, Mitra S
The interaction of thiocyanate with human native and cross-linked...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w
Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Related Articles Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Biochemistry. 2003 Sep 30;42(38):11100-8
Authors: Cai S, Stevens SY, Budor AP, Zuiderweg ER
The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillu
X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion.
Related Articles X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion.
Biochemistry. 2003 Mar 4;42(8):2467-74
Authors: Banci L, Bertini I, Del Conte R, Mangani S, Meyer-Klaucke W
XAS studies have been performed, under various experimental conditions, on a copper(I)-transporting protein, CopZ, of Bacillus subtilis....
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] NMR structure and metal interactions of the CopZ copper chaperone.
NMR structure and metal interactions of the CopZ copper chaperone.
Related Articles NMR structure and metal interactions of the CopZ copper chaperone.
J Biol Chem. 1999 Aug 6;274(32):22597-603
Authors: Wimmer R, Herrmann T, Solioz M, Wüthrich K
A recently discovered family of proteins that function as copper chaperones route copper to proteins that either require it for their function or are involved in its transport. In Enterococcus hirae the copper chaperone function is performed by the 8-kDa protein CopZ. This paper describes the NMR...
An NMR study of the interaction between the human copper(I) chaperone and the second
Linear Mode
