Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 433, Issue 4, Pages -Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2020.166788
Keywords
Rossmann-fold; minimal Rossmann-like motif; protein evolution; domains classification
Categories
Funding
- National Institutes of Health [GM127390]
- Welch Foundation [I-1505]
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The Rossmann-like fold is a prevalent and diversified double-helical superstructure of ancient evolutionary origin, present in various metabolic enzymes; RLM-containing proteins constitute approximately 15% of the human proteome, with disease-causing mutations more frequent within RLM domains, highlighting their importance for human health.
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. (C) 2020 Elsevier Ltd. All rights reserved.
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