| RRC ID |
52237
|
| 著者 |
Miyamoto K, Uechi A, Saito K.
|
| タイトル |
The zinc finger domain of RING finger protein 141 reveals a unique RING fold.
|
| ジャーナル |
Protein Sci
|
| 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 C3 HC4 -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.
|
| 巻・号 |
26(8)
|
| ページ |
1681-1686
|
| 公開日 |
2017-8-1
|
| DOI |
10.1002/pro.3201
|
| PMID |
28547869
|
| PMC |
PMC5521587
|
| MeSH |
Amino Acid Sequence
Binding Sites
Cations, Divalent
DNA-Binding Proteins / chemistry*
DNA-Binding Proteins / metabolism
Humans
Male
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Nuclear Proteins / chemistry*
Nuclear Proteins / metabolism
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
Sequence Alignment
Sequence Homology, Amino Acid
Spermatozoa / chemistry
Spermatozoa / metabolism
Thermodynamics
Zinc / chemistry*
|
| IF |
3.876
|
| 引用数 |
3
|
| リソース情報 |
| ヒト・動物細胞 |
Dnmt1-/-Dnmt3a-/-Dnmt3b-/- ES (clone19)(AES0146) |
