NMR paper An NMR study of the interaction between the human copper(I) chaperone and the second

		BioNMR > Educational resources > Journal club
[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

11-24-2010, 11:14 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,700

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

An NMR study of the interaction between the human copper(I) chaperone and the second

An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.

Related Articles An 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.

PMID: 15670166 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
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...	nmrlearner	Journal club	0	11-18-2010 08:31 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off