Fold combinations in multi-domain proteins.
domain architecture
domain folds
multi-domain proteins
protein evolution
protein structure
Journal
Bioinformation
ISSN: 0973-2063
Titre abrégé: Bioinformation
Pays: Singapore
ID NLM: 101258255
Informations de publication
Date de publication:
2019
2019
Historique:
received:
05
05
2019
accepted:
07
05
2019
entrez:
29
6
2019
pubmed:
30
6
2019
medline:
30
6
2019
Statut:
epublish
Résumé
Domain-domain interactions in multi-domain proteins play an important role in the combined function of individual domains for the overall biological activity of the protein. The functions of the tethered domains are often coupled and hence, limited numbers of domain architectures with defined folds are known in nature. Therefore, it is of interest to document the available fold-fold combinations and their preference in multi-domain proteins. Hence, we analyzed all multi-domain proteins with known structures in the protein databank and observed that only about 860 fold-fold combinations are present among them. Analyses of multi-domain proteins represented in sequence database result in recognition of 29,860 fold-fold combinations and it accounts for only 2.8% of the theoretically possible 1,036,080 (1439C2) fold-fold combinations. The observed preference for fold-fold combinations in multi-domain proteins is interesting in the context of multiple functions through structural adaptation by gene fusion.
Identifiants
pubmed: 31249437
doi: 10.6026/97320630015342
pii: 97320630015342
pmc: PMC6589474
doi:
Types de publication
Journal Article
Langues
eng
Pagination
342-350Références
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