The zinc finger domain of RING finger protein 141 reveals a unique RING fold

Miyamoto, Kazuhide; Uechi, Airi; Saito, Kazuki

doi:10.1002/pro.3201

Cited by 6 publications

(3 citation statements)

References 37 publications

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“…Of these, the most prevalent are the zinc finger proteins that are representative of flexible proteins that are stabilized via metal-binding. Short and longer peptides have been used extensively for modeling and understanding different aspects of zinc finger binding, including metal coordination, folding and actual binding [120][121][122]: Cyclic peptides with linear tails showed conformational and thermodynamic stability relative to linear peptides for modeling zinc fingers, and were able to fold into conformations that reproduced the zinc-ribbon fold of zinc fingers and bound Zn(II) better than their linear counterparts [123]. Peptides were used to study secondary structural elements common in zinc fingers and their role in folding and binding zinc: This enabled designing peptides that were modified by 23% of their native residues and still showed tertiary folds and stability on par with the natural backbone of the original zinc finger protein [124].…”

Section: Zincmentioning

confidence: 99%

Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

Shalev

2022

IJMS

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Metal chelation can provide structural stability and form reactive centers in metalloproteins. Approximately one third of known protein structures are metalloproteins, and metal binding, or the lack thereof, is often implicated in disease, making it necessary to be able to study these systems in detail. Peptide-metal complexes are both present in nature and can provide a means to focus on the binding region of a protein and control experimental variables to a high degree. Structural studies of peptide complexes with metal ions by nuclear magnetic resonance (NMR) were surveyed for all the essential metal complexes and many non-essential metal complexes. The various methods used to study each metal ion are presented together with examples of recent research. Many of these metal systems have been individually reviewed and this current overview of NMR studies of metallopeptide complexes aims to provide a basis for inspiration from structural studies and methodology applied in the field.

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Section: Zincmentioning

confidence: 99%

Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

Shalev

2022

IJMS

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“…The amino acid sequences of the EL5 RING finger and the SIAH1 RING finger are shown in Figure (A). The three‐dimensional structures of several RING fingers have been reported by using NMR methods and X‐ray diffraction . The RING finger structures bind to two zinc atoms and all have the essential active site corresponding to the amino acid sequence between the sixth and the seventh zinc‐binding residues.…”

Section: Molecular Design Strategy Of Artificial Ring Fingers (Arfs)mentioning

confidence: 99%

Concise machinery for monitoring ubiquitination activities using novel artificial RING fingers

Miyamoto

Saito

2018

Protein Science

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Protein ubiquitination is involved in many cellular processes, such as protein degradation, DNA repair, and signal transduction pathways. Ubiquitin-conjugating (E2) enzymes of the ubiquitination pathway are associated with various cancers, such as leukemia, lung cancer, and gastric cancer. However, to date, detection of E2 activities is not practicable for capturing the pathological conditions of cancers due to complications related to the enzymatic cascade reaction. To overcome this hurdle, we have recently investigated a novel strategy for measuring E2 activities. Artificial RING fingers (ARFs) were developed to conveniently detect E2 activities during the ubiquitination reaction. ARFs were created by grafting the active sites of ubiquitin-ligating (E3) enzymes onto amino acid sequences with 38 residues. The grafting design downsized E3s to small molecules (ARFs). Such an ARF is a multifunctional molecule that possesses specific E2-binding capabilities and ubiquitinates itself without a substrate. In this review, we discuss the major findings from recent investigations on a new molecular design for ARFs and their simplified detection system for E2 activities. The use of the ARF allowed us to monitor E2 activities using acute promyelocytic leukemia (APL)-derived cells following treatment with the anticancer drug bortezomib. The molecular design of ARFs is extremely simple and convenient, and thus, may be a powerful tool for protein engineering. The ARF methodology may reveal a new screening method of E2s that will contribute to diagnostic techniques for cancers.

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“…To unravel the intricacies of zinc finger binding, both short and longer peptides have been extensively utilized. These peptides serve as invaluable tools for modeling various aspects of zinc finger behavior, including metal coordination, folding dynamics, and actual binding processes [ 69 , 70 , 71 , 72 ]. Figure 13 gives a comparison between the α-peptide and oligourea backbones, as well as an illustration of the structures.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Biological Activities of Some Metal Complexes of Peptides: A Review

Marinova,

Tamahkyarova

2024

BioTech

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Peptides, both natural and synthetic, are well suited for a wide range of purposes and offer versatile applications in different fields such as biocatalysts, injectable hydrogels, tumor treatment, and drug delivery. The research of the better part of the cited papers was conducted using various database platforms such as MetalPDB. The rising prominence of therapeutic peptides encompasses anticancer, antiviral, antimicrobial, and anti-neurodegenerative properties. The metals Na, K, Mg, Ca, Fe, Mn, Co, Cu, Zn, and Mo are ten of the twenty elements that are considered essential for life. Crucial for understanding the biological role of metals is the exploration of metal-bound proteins and peptides. Aside from essential metals, there are other non-essential metals that also interact biologically, exhibiting either therapeutic or toxic effects. Irregularities in metal binding contribute to diseases like Alzheimer’s, neurodegenerative disorders, Wilson’s, and Menkes disease. Certain metal complexes have potential applications as radiopharmaceuticals. The examination of these complexes was achieved by preforming UV–Vis, IR, EPR, NMR spectroscopy, and X-ray analysis. This summary, although unable to cover all of the studies in the field, offers a review of the ongoing experimentation and is a basis for new ideas, as well as strategies to explore and gain knowledge from the extensive realm of peptide-chelated metals and biotechnologies.

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The zinc finger domain of RING finger protein 141 reveals a unique RING fold

Cited by 6 publications

References 37 publications

Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

Concise machinery for monitoring ubiquitination activities using novel artificial RING fingers

Synthesis and Biological Activities of Some Metal Complexes of Peptides: A Review

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