scholarly journals The role of copper(ii) in the aggregation of human amylin

Metallomics ◽  
2014 ◽  
Vol 6 (10) ◽  
pp. 1841-1852 ◽  
Author(s):  
Alessandro Sinopoli ◽  
Antonio Magrì ◽  
Danilo Milardi ◽  
Matteo Pappalardo ◽  
Pietro Pucci ◽  
...  
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Model Peptide ◽  
Metal Binding Site ◽  
Human Amylin

Copper(ii) coordination to human amylin has an influence on the aggregation and cytotoxic features of the polypeptide. Comparative investigations, carried out on a model peptide encompassing the 17–29 aminoacid region of amylin containing the putative metal binding site, support the non-fibrillar nature of the copper(ii) complexes.

scholarly journals Hybrid QM/MM Simulations Confirm Zn(II) Coordination Sphere That Includes Four Cysteines from the P2 × 4R Head Domain

2021 ◽  
Vol 22 (14) ◽  
pp. 7288
Author(s):  
Francisco Andrés Peralta ◽  
J. Pablo Huidobro-Toro ◽  
Raúl Mera-Adasme
Keyword(s):  
Binding Site ◽  
Coordination Sphere ◽  
Metal Binding ◽  
Metal Ion ◽  
Dynamic Simulations ◽  
Metal Binding Site ◽  
Head Domain ◽  
Water Ligands ◽  
Role Of Zn

To ascertain the role of Zn(II) as an allosteric modulator on P2X4R, QM/MM molecular dynamic simulations were performed on the WT and two P2X4R mutants suggested by previous electrophysiological data to affect Zn(II) binding. The Gibbs free energy for the reduction of the putative P2X4R Zn(II) binding site by glutathione was estimated at −22 kcal/mol. Simulations of the WT P2X4R head domain revealed a flexible coordination sphere dominated by an octahedral geometry encompassing C126, N127, C132, C149, C159 and a water molecule. The C132A mutation disrupted the metal binding site, leading to a coordination sphere with a majority of water ligands, and a displacement of the metal ion towards the solvent. The C132A/C159A mutant exhibited a tendency towards WT-like stability by incorporating the R148 backbone to the coordination sphere. Thus, the computational findings agree with previous experimental data showing Zn(II) modulation for the WT and C132A/C159A variants, but not for the C132A mutant. The results provide molecular insights into the nature of the Zn(II) modulation in P2X4R, and the effect of the C132A and C132A/C159A mutations, accounting for an elusive modulation mechanism possibly occurring in other extracellular or membrane protein.

scholarly journals Reduced quenching effect of pyridine ligands in highly luminescent Ln(III) complexes: the role of tertiary amide linkers

2021 ◽  
Author(s):  
Daniel Kocsi ◽  
Daniel Kovacs ◽  
Jordann A. L. Wells ◽  
Eszter Borbas
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
Quenching Effect ◽  
Pyridine Ligands ◽  
Tertiary Amide

Luminescent Eu(III) and Tb(III) complexes were synthesised from octadentate ligands carrying various carbostyril sensitizing antennae and two bidentate picolinate donors. Antennae were connected to the metal binding site via tertiary...

scholarly journals Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B

2005 ◽  
Vol 14 (11) ◽  
pp. 2828-2837 ◽  
Author(s):  
Alexandre Olry ◽  
Sandrine Boschi-Muller ◽  
Hong Yu ◽  
Daniel Burnel ◽  
Guy Branlant
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site

A metal-binding site in the RTN1-C protein: new perspectives on the physiological role of a neuronal protein

Metallomics ◽  
2012 ◽  
Vol 4 (5) ◽  
pp. 480 ◽  
Author(s):  
Ridvan Nepravishta ◽  
Francesca Polizio ◽  
Maurizio Paci ◽  
Sonia Melino
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Physiological Role ◽  
Metal Binding Site ◽  
C Protein ◽  
Neuronal Protein

scholarly journals The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jie Sheng ◽  
Bart M. Gadella ◽  
Nick K. Olrichs ◽  
Dora V. Kaloyanova ◽  
J. Bernd Helms
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Protein Complexes ◽  
Secretory Proteins ◽  
Protein Oligomerization ◽  
Functional Protein ◽  
Metal Binding Site ◽  
Mammalian Fertilization

AbstractCysteine-rich secretory proteins (CRISPs) are a subgroup of the CRISP, antigen 5 and PR-1 (CAP) superfamily that is characterized by the presence of a conserved CAP domain. Two conserved histidines in the CAP domain are proposed to function as a Zn2+-binding site with unknown function. Human CRISP1 is, however, one of the few family members that lack one of these characteristic histidine residues. The Zn2+-dependent oligomerization properties of human CRISP1 were investigated using a maltose-binding protein (MBP)-tagging approach in combination with low expression levels in XL-1 Blue bacteria. Moderate yields of soluble recombinant MBP-tagged human CRISP1 (MBP-CRISP1) and the MBP-tagged CAP domain of CRISP1 (MBP-CRISP1ΔC) were obtained. Zn2+ specifically induced oligomerization of both MBP-CRISP1 and MBP-CRISP1ΔC in vitro. The conserved His142 in the CAP domain was essential for this Zn2+ dependent oligomerization process, confirming a role of the CAP metal-binding site in the interaction with Zn2+. Furthermore, MBP-CRISP1 and MBP-CRISP1ΔC oligomers dissociated into monomers upon Zn2+ removal by EDTA. Condensation of proteins is characteristic for maturing sperm in the epididymis and this process was previously found to be Zn2+-dependent. The Zn2+-induced oligomerization of human recombinant CRISP1 may shed novel insights into the formation of functional protein complexes involved in mammalian fertilization.

Unraveling the Substrate−Metal Binding Site of Ferrochelatase:  An X-ray Absorption Spectroscopic Study†

Biochemistry ◽  
2002 ◽  
Vol 41 (15) ◽  
pp. 4809-4818 ◽  
Author(s):  
Gloria C. Ferreira ◽  
Ricardo Franco ◽  
Arianna Mangravita ◽  
Graham N. George
Keyword(s):  
Spectroscopic Study ◽  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
X Ray ◽  
Substrate Metal ◽  
X Ray Absorption
Sign in / Sign up

Export Citation Format

Share Document