Amino Terminal Cu(II)- and Ni(II)-Binding (ATCUN) Motif of Proteins and Peptides:  Metal Binding, DNA Cleavage, and Other Properties

and, Catherine Harford‡; Sarkar, Bibudhendra

doi:10.1021/ar9501535

Cited by 480 publications

(584 citation statements)

References 64 publications

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“…DAHK (Asp-Ala-His-Lys) is the N-terminal metal binding sequence of human serum albumin (HSA) [9,10] which is the major protein in the blood and in the cerebrospinal fluid and is involved in Cu transport [11,12]. Cu 2+ is bound to the so called ATCUN motif [9], which is also found in many Scheme 1: Cu 2+ coordination of peptides with the N-terminal sequence Xxx-Xxx-His (ATCUN motive like DAHK) (left) and Xxx-His (like GHK) (right).…”

Section: Introductionmentioning

confidence: 99%

“…Cu 2+ is bound to the so called ATCUN motif [9], which is also found in many Scheme 1: Cu 2+ coordination of peptides with the N-terminal sequence Xxx-Xxx-His (ATCUN motive like DAHK) (left) and Xxx-His (like GHK) (right). GHK has an equatorial labile coordination position (X) and it can form ternary complexes.…”

Section: Introductionmentioning

confidence: 99%

“…Cu 2+ is bound in a slightly distorted square planar geometry by 4 nitrogen atoms: the N-terminal amine, the two amidyl functions from Asp-Ala and Ala-His peptide bonds and the N  from the imidazole ring of His (Scheme 1, left) [9].…”

Section: Introductionmentioning

confidence: 99%

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Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

et al. 2011

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The peptides Asp-Ala-His-Lys (DAHK) and Gly-His-Lys (GHK) are naturally occurring copper(II)-chelating motives in human serum and cerebrospinal fluid. Here the sensitive thermodynamic technique isothermal titration calorimetry (ITC) has been used to study the energetics of copper(II) binding to DAHK and GHK peptides in the presence of the weaker ligand glycine as a competitor. DAHK and GHK bind Cu(II) predominantly in a 1:1 stoichiometry with conditional dissociation constants (i.e. at pH 7.4, in the absence of the competing chelators glycine and HEPES buffer) of 2.6 +/-0.4 x 10 -14 M and of 7.0 +/-1.0 x 10 -14 M, respectively. Furthermore, the apparent ΔH values were measured and the number of protons released upon Cu(II) binding was determined by performing experiments in different buffers. This allowed us to determine the conditional ΔG, ΔH, and ΔS, i.e. corrected for the contributions of the weaker ligand glycine and the buffer at pH 7.4. We found that the entropic and enthalpic contributions to the Cu(II)-binding to GHK and DAHK are distinct, with a higher enthalpic contribution for GHK. The obtained thermodynamic parameters correspond well to those in the literature obtained by other techniques, suggesting that the use of the weaker ligand glycine as a competitor in ITC provides accurate data for Cu(II)-binding to high affinity peptides, which cannot be accurately determined without the use of a competitor ligand.3

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

et al. 2011

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“…However, in contrast to the consensus zinc binding motif of metalloproteinases [11], the histatin sequence contains many neighboring basic residues. A copper binding ATCUN motif is also located in the N-terminal region of histatins 3 and 5 [12].…”

Section: Introductionmentioning

confidence: 99%

Zinc and copper bind to unique sites of histatin 5

et al. 2001

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Metal binding has been suggested to be relevant in the antifungal and antibacterial mechanism of histatin 5, a human salivary protein. Proton nuclear magnetic resonance (NMR) spectra were obtained to investigate the specificity of metal binding to the seven histidyl, one aspartyl and one glutamyl amino acid side-chains of histatin 5 in aqueous solutions. Three C O1^H histidyl and the C Q^H glutamyl resonances of histatin 5 were selectively altered in spectra of solutions containing three equivalents of zinc. Copper binding to histatin 5 resulted in a reduced intensity of C L^H aspartyl resonances, while no evidence for calcium binding was found. These results indicate that zinc binding to histatin 5 involves His-15 present within the^H^E^XX^H^z inc binding motif, and copper binding occurs within the N-terminal D^S^H^, ATCUN motif. ß

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“…The Cu,Zn SODs of certain bacteria (e.g. H. parainfluenzae, H. influenzae, N. meningitidis) possess an N-terminal HxH sequence [8], a well-known high affinity copper(II) binding site (ATCUN motif) found in the N-terminus of several naturally occurring copper-binding proteins, such as human serum albumin [10]. Further interesting examples of such metal binding regions are present in the enzymes isolated from Haemophilus ducreyi and Actinobacillus pleuropneumoniae.…”

Section: Introductionmentioning

confidence: 99%

On the possible roles of N-terminal His-rich domains of Cu,Zn SODs of some Gram-negative bacteria

Árus

Jancsó

Szunyogh

et al. 2012

Journal of Inorganic Biochemistry

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Amino Terminal Cu(II)- and Ni(II)-Binding (ATCUN) Motif of Proteins and Peptides: Metal Binding, DNA Cleavage, and Other Properties

Cited by 480 publications

References 64 publications

Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

Zinc and copper bind to unique sites of histatin 5

On the possible roles of N-terminal His-rich domains of Cu,Zn SODs of some Gram-negative bacteria

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