NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
Chem Commun (Camb). 2011 Jun 14;47(22):6407-9
Authors: Shoshan MS, Shalev DE, Adriaens W, Merkx M, Hackeng TM, Tshuva EY
Abstract
The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ~3.0 and ~6.8 Cu(I) binds through one Cys and the Met...
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09-21-2011 03:31 PM
[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...
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12-01-2010 06:56 PM
[NMR paper] A strategy for the NMR characterization of type II copper(II) proteins: the case of t
A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae.
Related Articles A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae.
J Am Chem Soc. 2003 Jun 18;125(24):7200-8
Authors: Arnesano F, Banci L, Bertini I, Felli IC, Luchinat C, Thompsett AR
CopC from Pseudomonas syringae was found to be a protein capable of binding both Cu(I) and Cu(II) at two different...
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11-24-2010 09:01 PM
[NMR paper] Characterization of the monomeric form of the transmembrane and cytoplasmic domains o
Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy.
Related Articles Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy.
Biochemistry. 2002 Dec 31;41(52):15618-24
Authors: Li R, Babu CR, Valentine K, Lear JD, Wand AJ, Bennett JS, DeGrado WF
We have characterized a membrane protein containing residues P688-T762 of the integrin beta3 subunit, encompassing its transmembrane and...
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11-24-2010 08:58 PM
[NMR paper] Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a no
Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a novel 1H NMR spectrum of a 'Tri-Cu(II)' center in protein.
Related Articles Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a novel 1H NMR spectrum of a 'Tri-Cu(II)' center in protein.
J Inorg Biochem. 2001 Dec 1;87(3):149-56
Authors: Epperson JD, Ming LJ
The phosphatidylcholine-preferring phospholipase C from Bacillus cereus (PC-PLC(Bc)) is a tri-Zn enzyme with two 'tight binding' and one 'loose binding' sites. The Zn2+ ions can...
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11-19-2010 08:44 PM
[NMR paper] Electronic characterization of the oxidized state of the blue copper protein rusticya
Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?
Related Articles Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?
Biochemistry. 2001 Jan 23;40(3):837-46
Authors: Donaire A, Jiménez B, Moratal J, Hall JF, Hasnain SS
The oxidized state of rusticyanin, the blue copper protein with the highest...
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11-19-2010 08:32 PM
NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Related Articles NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Biochemistry. 2010 Aug 27;
Authors: Fatemi N, Korzhnev DM, VÄ?lyvis A, Sarkar B, Forman-Kay JD
The Wilson disease protein (ATP7B) is a copper-transporting member of the P-type ATPase superfamily, which plays a central role in copper homeostasis and interacts with the copper chaperone Atox1. The N-terminus of ATP7B is comprised of six copper-binding domains (WCBDs), each capable of binding one copper atom in the...
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08-31-2010 09:42 PM
NMR characterization of foldedness for the production of E3 RING domains.
NMR characterization of foldedness for the production of E3 RING domains.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR characterization of foldedness for the production of E3 RING domains.
J Struct Biol. 2010 Aug 2;
Authors: Huang A, de Jong RN, Folkers GE, Boelens R
We summarize the use of NMR spectroscopy in the production and the screening of stability and foldedness of protein domains, and apply it to the RING domains of E3 ubiquitin-ligases. RING domains...
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
Linear Mode
