Not an exception to the rule: the functional significance of intrinsically disordered protein regions in enzymes
Author:
Affiliation:
1. Department of Molecular Medicine
2. Morsani College of Medicine
3. University of South Florida
4. Tampa
5. USA
Abstract
Analysis of the PDB and 66 proteomes revealed that disordered regions in enzymes occur at similar lengths and frequencies as in non-enzymes.
Funder
Russian Science Foundation
Publisher
Royal Society of Chemistry (RSC)
Subject
Molecular Biology,Biotechnology
Link
http://pubs.rsc.org/en/content/articlepdf/2017/MB/C6MB00741D
Reference38 articles.
1. Disorder Targets Misorder in Nuclear Quality Control Degradation: A Disordered Ubiquitin Ligase Directly Recognizes Its Misfolded Substrates
2. A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites
3. Intrinsic disorder drives N-terminal ubiquitination by Ube2w
4. A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1
5. The Disordered C-Terminal Domain of Human DNA Glycosylase NEIL1 Contributes to Its Stability via Intramolecular Interactions
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