serval:BIB_B15CF13C8D83
In Search of Functional Advantages of Knots in Proteins.
10.1371/journal.pone.0165986
000386715500076
27806097
Dabrowski-Tumanski
P.
author
Stasiak
A.
author
Sulkowska
J.I.
author
article
2016
PLoS One
1932-6203
1932-6203
journal
11
11
e0165986
We analysed the structure of deeply knotted proteins representing three unrelated families of knotted proteins. We looked at the correlation between positions of knotted cores in these proteins and such local structural characteristics as the number of intra-chain contacts, structural stability and solvent accessibility. We observed that the knotted cores and especially their borders showed strong enrichment in the number of contacts. These regions showed also increased thermal stability, whereas their solvent accessibility was decreased. Interestingly, the active sites within these knotted proteins preferentially located in the regions with increased number of contacts that also have increased thermal stability and decreased solvent accessibility. Our results suggest that knotting of polypeptide chains provides a favourable environment for the active sites observed in knotted proteins. Some knotted proteins have homologues without a knot. Interestingly, these unknotted homologues form local entanglements that retain structural characteristics of the knotted cores.
eng
60_published
true
peer-reviewed
University of Lausanne
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