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

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 reson...

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Bibliographic Details
Published in:Protein science 2017-08, Vol.26 (8), p.1681-1686
Main Authors: Miyamoto, Kazuhide, Uechi, Airi, Saito, Kazuki
Format: Article
Language:English
Subjects:
Amino Acid Sequence
artificial RING finger
Atomic structure
Binding Sites
Cations, Divalent
Chemical modification
Cysteine
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Humans
Male
Models, Molecular
Modular structures
NMR
NMR structure
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Nuclear Proteins - chemistry
Nuclear Proteins - metabolism
peptide
Peptides
Peptides - chemical synthesis
Peptides - chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Domains
Protein Folding
Protein Isoforms - chemistry
Protein Isoforms - metabolism
Protein Structure Reports
RING finger protein 141
Sequence Alignment
Sequence Homology, Amino Acid
Spermatogenesis
Spermatozoa - chemistry
Spermatozoa - metabolism
Structural analysis
Thermodynamics
Ubiquitin
Ubiquitin-conjugating enzyme
Zinc
Zinc - chemistry
zinc finger
Zinc finger proteins
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Summary: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 C3HC4‐type RING fold. The position and range of the helical active site of the RFP141C structure were elucidated at the atomic level. Therefore, structural analysis may allow RFP141C to be used for designing an artificial RING finger possessing specific ubiquitin‐conjugating enzyme (E2)‐binding capabilities. PDB Code(s): 5XEK
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.3201