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AlphaFold2 reveals commonalities and novelties in protein structure space for 21 model organisms
Cited 19 time in
Web of Science
Cited 23 time in Scopus
- Authors
- Issue Date
- 2023-02
- Publisher
- Nature Publishing Group
- Citation
- Communications Biology, Vol.6 No.1, p. 160
- Abstract
- Deep-learning (DL) methods like DeepMind's AlphaFold2 (AF2) have led to substantial improvements in protein structure prediction. We analyse confident AF2 models from 21 model organisms using a new classification protocol (CATH-Assign) which exploits novel DL methods for structural comparison and classification. Of similar to 370,000 confident models, 92% can be assigned to 3253 superfamilies in our CATH domain superfamily classification. The remaining cluster into 2367 putative novel superfamilies. Detailed manual analysis on 618 of these, having at least one human relative, reveal extremely remote homologies and further unusual features. Only 25 novel superfamilies could be confirmed. Although most models map to existing superfamilies, AF2 domains expand CATH by 67% and increases the number of unique 'global' folds by 36% and will provide valuable insights on structure function relationships. CATH-Assign will harness the huge expansion in structural data provided by DeepMind to rationalise evolutionary changes driving functional divergence.
- ISSN
- 2399-3642
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