Ontology highlight
ABSTRACT:
SUBMITTER: Virnau P
PROVIDER: S-EPMC1570178 | biostudies-literature | 2006 Sep
REPOSITORIES: biostudies-literature
Virnau Peter P Mirny Leonid A LA Kardar Mehran M
PLoS computational biology 20060728 9
Our investigation of knotted structures in the Protein Data Bank reveals the most complicated knot discovered to date. We suggest that the occurrence of this knot in a human ubiquitin hydrolase might be related to the role of the enzyme in protein degradation. While knots are usually preserved among homologues, we also identify an exception in a transcarbamylase. This allows us to exemplify the function of knots in proteins and to suggest how they may have been created. ...[more]