Influence of the proline residue on the co-ordination of Cu(II) to peptides containing -Pro- and -Pro-Pro- subunits

Pettit, Leslie D.; Livera, C.; Steel, Ian; Bataille, Michel; Cardon, C.; Formicka-Kozlowska, Grazyna

doi:10.1016/s0277-5387(00)81237-1

Cited by 8 publications

(8 citation statements)

References 17 publications

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“…Proline residue in the second position preceding anchoring histidine residue in proteins with His 3 prevents binding of Cu(II) in a studied here manner. This results from the lack of proton, exchangeable with the copper ion, in the tertiary amide in the polypeptide chain with proline [11,23] . Such proline residue was labeled as a ‘break‐point’ in the ATCUN sequences (with His 3 ) [11,23] .…”

Section: Resultsmentioning

confidence: 99%

“…This results from the lack of proton, exchangeable with the copper ion, in the tertiary amide in the polypeptide chain with proline [11,23] . Such proline residue was labeled as a ‘break‐point’ in the ATCUN sequences (with His 3 ) [11,23] . In this case, there is no coordination‐favoring advantage of simultaneous anchoring by histidine imidazole and free amine nitrogen in the N‐terminal Cu(II) binding.…”

Section: Resultsmentioning

confidence: 99%

“…Regardless, there are only 26 such additional sequences in human matured proteins ( Tables S5 and S7 ) and 5 in propeptides/signal peptides ( Tables S11 and S12 ). Importantly, proline residue in the first position of proteins/peptides with His 2 and His 3 binds Cu(II) similarly to other amino acid residues [11,23] …”

Section: Resultsmentioning

confidence: 99%

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Cu(II)‐Binding N‐Terminal Sequences of Human Proteins

Frączyk

2021

Chemistry & Biodiversity

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Proteins anchor copper(II) ions mainly by imidazole from histidine residues located in different positions in the primary protein structures. However, the motifs with histidine in the first three N‐terminal positions (His1, His2, and His3) show unique Cu(II)‐binding properties, such as availability from the surface of the protein, high flexibility, and high Cu(II) exchangeability with other ligands. It makes such sequences beneficial for the fast exchange of Cu(II) between ligands. Furthermore, sequences with His1 and His2, thus, non‐saturating the Cu(II) coordination sphere, are redox‐active and may play a role in Cu(II) reduction to Cu(I). All human protein sequences deposited in UniProt Knowledgebase were browsed for those containing His1, His2, or His3. Proteolytically modified sequences (with the removal of a propeptide or Met residue) were taken for the analysis. Finally, the sequences were sorted out according to the subcellular localization of the proteins to match the respective sequences with the probability of interaction with divalent copper.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Cu(II)‐Binding N‐Terminal Sequences of Human Proteins

Frączyk

2021

Chemistry & Biodiversity

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“…In Pro peptides, the second proline nitrogen atom in the peptide backbone is unable to undergo ionization and participate in the formation of the N − → Cu(II) bond. Therefore, it acts as a "break-point" in metal coordination [50][51][52][53]. The characteristic feature of the tetrazole moiety distinguishing it from the Pro residue is the presence of N(4) nitrogen atom as a potential donor center for a metal ion (Scheme 2).…”

Section: Copper(ii) Complexes With the Tetrazole Analogue Of Tetraalamentioning

confidence: 99%

Tetrazole peptides as copper(II) ion chelators

Łodyga-Chruścińska¹

2011

Coordination Chemistry Reviews

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“…There is an enormous structural variety for the complex formation of prolyl and weakly or strongly coordinating side chain residues [248][249][250][251][252]. The most interesting feature of systems containing proline residues is the induction of large macrochelate loops formation, with Cu 2+ bound to the N-terminal amino group and a distance donor.…”

Section: Impact Of Proline On Peptide Coordination Abilitiesmentioning

confidence: 99%

Study of the mechanisms of toxicity and carcinogenicity induced by metal ions

Nunes¹

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European Social Fund), with the title "Study of the mechanisms of toxicity and carcinogenicity induced by metal ions" and coordinated by Prof. Nick Hadjiliadis. The subject of the thesis was given to me by Prof. N. Hadjiliadis and the thesis was performed mainly in his laboratory.I would like therefore, first to thank Prof. Nick Hadjiliadis, my supervisor, for the opportunity he gave me, by organizing every step of the thesis, the support both financial and scientific, and guidance and in summary for providing me with all necessary tools for the development and successful ending of this work.

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Influence of the proline residue on the co-ordination of Cu(II) to peptides containing -Pro- and -Pro-Pro- subunits

Cited by 8 publications

References 17 publications

Cu(II)‐Binding N‐Terminal Sequences of Human Proteins

Cu(II)‐Binding N‐Terminal Sequences of Human Proteins

Tetrazole peptides as copper(II) ion chelators

Study of the mechanisms of toxicity and carcinogenicity induced by metal ions

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