Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins-Reference-Cited by-同舟云学术

Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins

Published:2018-10-05 Issue:10 Volume:4 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Jemth Per¹^ORCID,Karlsson Elin¹,Vögeli Beat²^ORCID,Guzovsky Brenda³,Andersson Eva¹,Hultqvist Greta⁴^ORCID,Dogan Jakob⁵,Güntert Peter⁶⁷⁸^ORCID,Riek Roland⁶,Chi Celestine N.¹^ORCID

Affiliation:

1. Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123 Uppsala, Sweden.

2. Department of Biochemistry and Molecular Genetics, University of Colorado at Denver, 12801 East 17th Avenue, Aurora, CO 80045, USA.

3. Protein Physiology Lab, FCEyN-Universidad de Buenos Aires, IQUIBICEN/CONICET, Intendente Güiraldes 2160, Ciudad Universitaria, C1428EGA Buenos Aires, Argentina.

4. Department of Pharmaceutical Biosciences, Uppsala University, BMC Box 591, SE-75124 Uppsala, Sweden.

5. Department of Biochemistry and Biophysics, Stockholm University, SE-10691 Stockholm, Sweden.

6. Laboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zürich, Switzerland.

7. Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, Goethe University, 60438 Frankfurt am Main, Germany.

8. Graduate School of Science, Tokyo Metropolitan University, Tokyo 192-0397, Japan.

Abstract

Structural snapshots characterize six hundred million years of evolution of intrinsically disordered proteins.

Funder

Wenner-Gren Foundation

University of Colorado Denver

Swedish Research Council Formas

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference39 articles.

1. The SRC family of nuclear receptor coactivators;Leo C.;Gene,2000

2. Evolutionary biochemistry: revealing the historical and physical causes of protein properties

3. Evolution of DNA specificity in a transcription factor family produced a new gene regulatory module;McKeown A. N.;Cell,2014

4. Evolutionary trend toward kinetic stability in the folding trajectory of RNases H;Lim S. A.;Proc. Natl. Acad. Sci. U.S.A.,2016

5. Evolutionary drivers of thermoadaptation in enzyme catalysis;Nguyen V.;Science,2017

Cited by 35 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Conformational entropy in molecular recognition of intrinsically disordered proteins;Current Opinion in Structural Biology;2023-12

2. The molecular basis for cellular function of intrinsically disordered protein regions;Nature Reviews Molecular Cell Biology;2023-11-13

3. Evolution of a plant growth-regulatory protein interaction specificity;Nature Plants;2023-10-30

4. Intrinsically Disordered Flanking Regions Increase the Affinity of a Transcriptional Coactivator Interaction across Vertebrates;Biochemistry;2023-08-30

5. IFF: Identifying key residues in intrinsically disordered regions of proteins using machine learning;Protein Science;2023-08-22