Document Type
Article
Publication Date
8-6-2019
Abstract
The origin of protein backbone threading through a topological knot remains elusive. To understand the evolutionary origin of protein knots, in this issue of StructureKo et al. (2019) used circular permutation to untie a knotted protein. They showed that a domain-swapped dimer releases the knot and the associated high-energy state for substrate binding.
Recommended Citation
Yin, Sitao; Dhital, Brittiny; and Hou, Ya-Ming, "How to Untie a Protein Knot." (2019). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 157.
https://jdc.jefferson.edu/bmpfp/157
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
PubMed ID
31390544
Language
English
Comments
This article has been peer reviewed. It is the authors' final version prior to publication in Structure, Volume 27, Issue 8, August 2019, Pages 1190-1191.
The published version is available at https://doi.org/10.1016/j.str.2019.07.008. Copyright © Elsevier