ArticleProtein science : a publication of the Protein Society2017
The zinc finger domain of RING finger protein 141 reveals a unique RING fold.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Synthesis and Biological Activities of Some Metal Complexes of Peptides: A Review.Biotech (Basel (Switzerland)) · 2024Review
- Studying Peptide-Metal Ion Complex Structures by Solution-State NMR.International journal of molecular sciences · 2022Review
- Article
- Prenatal androgen exposure and transgenerational susceptibility to polycystic ovary syndrome.Nature medicine · 2019Article
- Concise machinery for monitoring ubiquitination activities using novel artificial RING fingers.Protein science : a publication of the Protein Society · 2018Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human RING finger protein 141 (RFP141) is a germ cell-specific transcription factor during spermatogenesis. We synthesized a compact construct encoding the C-terminal zinc finger of RFP141 (RFP141C peptide). Herein we determined the solution structure of the RFP141C peptide by nuclear magnetic resonance (NMR). Moreover, NMR data and the chemical modification of cysteine residues demonstrated that the RFP141C peptide binds to two zinc atoms in a cross-brace arrangement. The Simple Modular Architecture Research Tool database predicted the structure of RFP141C as a RING finger. However, the actual structure of the RFP141C peptide adopts an atypical compact C
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