The large family of PC4-like domains - similar folds and functions throughout all kingdoms of life.
Animals
Binding Sites
Biological Evolution
DNA
/ chemistry
DNA-Binding Proteins
/ chemistry
Databases, Genetic
Humans
Models, Molecular
Protein Conformation
Protein Domains
Protein Folding
Protein Multimerization
RNA
/ chemistry
RNA-Binding Motifs
RNA-Binding Proteins
/ chemistry
Structure-Activity Relationship
KH-domain
PC4-like
PURA
RNA/DNA binding
RRM
protein domain
protein fold
structural biology
topology
Journal
RNA biology
ISSN: 1555-8584
Titre abrégé: RNA Biol
Pays: United States
ID NLM: 101235328
Informations de publication
Date de publication:
09 2020
09 2020
Historique:
pubmed:
2
6
2020
medline:
8
7
2021
entrez:
2
6
2020
Statut:
ppublish
Résumé
RNA- and DNA-binding domains are essential building blocks for specific regulation of gene expression. While a number of canonical nucleic acid binding domains share sequence and structural conservation, others are less obviously linked by evolutionary traits. In this review, we describe a protein fold of about 150 aa in length, bearing a conserved β-β-β-β-α-linker-β-β-β-β-α topology and similar nucleic acid binding properties but no apparent sequence conservation. The same overall fold can also be achieved by dimerization of two proteins, each bearing a β-β-β-β-α topology. These proteins include but are not limited to the transcription factors PC4 and P24 from humans and plants, respectively, the human RNA-transport factor Pur-α (also termed PURA), as well as the ssDNA-binding SP_0782 protein from
Identifiants
pubmed: 32476604
doi: 10.1080/15476286.2020.1761639
pmc: PMC7549692
doi:
Substances chimiques
DNA-Binding Proteins
0
RNA-Binding Proteins
0
RNA
63231-63-0
DNA
9007-49-2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1228-1238Références
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