A Fifth of the Protein World: Rossmann-like Proteins as an Evolutionarily Successful Structural unit.
J Mol Biol
; 433(4): 166788, 2021 02 19.
Article
in En
| MEDLINE
| ID: mdl-33387532
ABSTRACT
The Rossmann-like fold is the most prevalent and diversified doubly-wound superfold of ancient evolutionary origin. Rossmann-like domains are present in a variety of metabolic enzymes and are capable of binding diverse ligands. Discerning evolutionary relationships among these domains is challenging because of their diverse functions and ancient origin. We defined a minimal Rossmann-like structural motif (RLM), identified RLM-containing domains among known 3D structures (20%) and classified them according to their homologous relationships. New classifications were incorporated into our Evolutionary Classification of protein Domains (ECOD) database. We defined 156 homology groups (H-groups), which were further clustered into 123 possible homology groups (X-groups). Our analysis revealed that RLM-containing proteins constitute approximately 15% of the human proteome. We found that disease-causing mutations are more frequent within RLM domains than within non-RLM domains of these proteins, highlighting the importance of RLM-containing proteins for human health.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Conformation
/
Proteins
/
Models, Molecular
/
Amino Acid Motifs
Limits:
Humans
Language:
En
Journal:
J Mol Biol
Year:
2021
Document type:
Article