Paramagnetic NMR study of Cu2+?IDA complex localization on a protein surface and its application to elucidate long distance information

NOMURA, M

doi:10.1016/s0014-5793(04)00478-8

Cited by 9 publications

(10 citation statements)

References 21 publications

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“…For example, Kojima’s group characterized the in vitro interaction between ubiquitin and copper by using electron paramagnetic resonance (EPR) approximation (Nomura et al, 2004). This study strongly suggested that Cu 2+ , as a part of one metal complex, is coordinated by ubiquitin with the participation of a histidine residue (his-68).…”

Section: Copper and Ubiquitin Proteasome Systemmentioning

confidence: 99%

“…This study strongly suggested that Cu 2+ , as a part of one metal complex, is coordinated by ubiquitin with the participation of a histidine residue (his-68). Other paramagnetic metals, such as Mn 2+ and Gd 3+ , did not coordinate specifically to his-68 present in ubiquitin sequence (Nomura et al, 2004). In fact, ubiquitin is retained to immobilized metal ion affinity chromatography (IMAC) resins complexed to Cu 2+ (Hemdan et al, 1989), where his-68 is critical for this binding.…”

Section: Copper and Ubiquitin Proteasome Systemmentioning

confidence: 99%

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Copper: from neurotransmission to neuroproteostasis

Opazo¹,

Greenough²,

Bush³

2014

Front. Aging Neurosci.

133

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Copper is critical for the Central Nervous System (CNS) development and function. In particular, different studies have shown the effect of copper at brain synapses, where it inhibits Long Term Potentation (LTP) and receptor pharmacology. Paradoxically, according to recent studies copper is required for a normal LTP response. Copper is released at the synaptic cleft, where it blocks glutamate receptors, which explain its blocking effects on excitatory neurotransmission. Our results indicate that copper also enhances neurotransmission through the accumulation of PSD95 protein, which increase the levels of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors located at the plasma membrane of the post-synaptic density. Thus, our findings represent a novel mechanism for the action of copper, which may have implications for the neurophysiology and neuropathology of the CNS. These data indicate that synaptic configuration is sensitive to transient changes in transition metal homeostasis. Our results suggest that copper increases GluA1 subunit levels of the AMPA receptor through the anchorage of AMPA receptors to the plasma membrane as a result of PSD-95 accumulation. Here, we will review the role of copper on neurotransmission of CNS neurons. In addition, we will discuss the potential mechanisms by which copper could modulate neuronal proteostasis (“neuroproteostasis”) in the CNS with focus in the Ubiquitin Proteasome System (UPS), which is particularly relevant to neurological disorders such as Alzheimer’s disease (AD) where copper and protein dyshomeostasis may contribute to neurodegeneration. An understanding of these mechanisms may ultimately lead to the development of novel therapeutic approaches to control metal and synaptic alterations observed in AD patients.

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Section: Copper and Ubiquitin Proteasome Systemmentioning

confidence: 99%

Section: Copper and Ubiquitin Proteasome Systemmentioning

confidence: 99%

Copper: from neurotransmission to neuroproteostasis

Opazo¹,

Greenough²,

Bush³

2014

Front. Aging Neurosci.

133

View full text Add to dashboard Cite

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“…In the studies of a-synuclein and prion proteins, as well as in other studies [140,141,166,167,177,178], the location of the Cu 2+ ions was identified through the paramagnetic broadening (R 2p ) of the NMR signals of the nuclei spatially close to the metal-binding sites. However, this approach does not provide information that is sufficiently detailed for a precise determination of the location and the characteristics of the metalbinding sites.…”

Section: Thioredoxinmentioning

confidence: 99%

Investigating metal-binding in proteins by nuclear magnetic resonance

Jensen

Hass

Hansen

et al. 2007

Cell. Mol. Life Sci.

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Metal ions play a key role for the function of many proteins. The interaction of the metal ion with the protein and its involvement in the function of the protein vary widely. In some proteins, the metal ion is bound tightly to the ligand residues and may be the key player in the function of the protein, as in the case of blue copper proteins. In other proteins, the metal ion is bound only temporarily and loosely to the protein, as in the case of some metalloenzymes and other proteins where the metal ion acts as a cofactor necessary for the function of the protein. Such proteins are often known as metal ion-activated proteins. The review focuses on recent nuclear magnetic resonance (NMR) studies of a series of metal-dependent proteins and the characterization of the metal-binding sites. In particular, we focus on NMR techniques for studying metal binding to proteins such as chemical shift mapping, paramagnetic NMR and changes in backbone dynamics upon metal binding.

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“…The His-tag typically consists of five or six consecutive His residues added to the C-or N-terminus of the protein [20]. The most popular systems for oriented immobilization of His-tagged proteins are complexes of nitrilotriacetic acid (NTA) or iminodiacetic acid (IDA) with transition metal ions (Ni 2+ , Cu 2+ ) [20][21][22][23][24][25][26][27][28]. Nitrilotriacetic acid forms a tetradentatechelate with Ni 2+ and Cu 2+ , which is able to bind His-tagged proteins via coordinated bonds [29].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes

Kurzątkowska¹,

Mielecki²,

Grzelak³

et al. 2014

Talanta

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New surface plasmon resonance (SPR) sensing platform swhich consists of copper (II) complexes of a pentetic acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His 6 -JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His 6 -JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.

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Paramagnetic NMR study of Cu2+?IDA complex localization on a protein surface and its application to elucidate long distance information

Cited by 9 publications

References 21 publications

Copper: from neurotransmission to neuroproteostasis

Copper: from neurotransmission to neuroproteostasis

Investigating metal-binding in proteins by nuclear magnetic resonance

Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes

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