Biomaterial Database

The zinc finger domain of RING finger protein 141 reveals a unique RING fold. 2017

Kazuhide Miyamoto, and Airi Uechi, and Kazuki Saito

Department of Pharmaceutical Health Care, Faculty of Pharmaceutical Sciences, Himeji Dokkyo University, Hyogo, Japan.

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.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D009687	Nuclear Proteins	Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.	Nucleolar Protein,Nucleolar Proteins,Nuclear Protein,Protein, Nuclear,Protein, Nucleolar,Proteins, Nuclear,Proteins, Nucleolar
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D002413	Cations, Divalent	Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis.	Divalent Cations
D004268	DNA-Binding Proteins	Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.	DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000072417	Protein Domains	Discrete protein structural units that may fold independently of the rest of the protein and have their own functions.	Peptide Domain,Protein Domain,Domain, Peptide,Domain, Protein,Domains, Peptide,Domains, Protein,Peptide Domains
D000072756	Protein Conformation, alpha-Helical	A secondary structure of proteins that is a right-handed helix or coil, where each amino (N-H) group of the peptide backbone contributes a hydrogen bond to the carbonyl(C	alpha-Helical Conformation, Protein,alpha-Helical Protein Conformation,alpha-Helical Structures,alpha-Helices,alpha-Helix,Conformation, Protein alpha-Helical,Conformation, alpha-Helical Protein,Conformations, Protein alpha-Helical,Conformations, alpha-Helical Protein,Protein Conformation, alpha Helical,Protein Conformations, alpha-Helical,alpha Helical Conformation, Protein,alpha Helical Protein Conformation,alpha Helical Structures,alpha Helices,alpha Helix,alpha-Helical Conformations, Protein,alpha-Helical Protein Conformations,alpha-Helical Structure