Structural and Kinetic Characterization of the Intrinsically Disordered Protein SeV NTAIL through Enhanced Sampling Simulations

2017 ◽  
Vol 121 (41) ◽  
pp. 9572-9582 ◽  
Author(s):  
Mattia Bernetti ◽  
Matteo Masetti ◽  
Fabio Pietrucci ◽  
Martin Blackledge ◽  
Malene Ringkjobing Jensen ◽  
...  
2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Na Liu ◽  
Yue Guo ◽  
Shangbo Ning ◽  
Mojie Duan

Abstract Phosphorylation is one of the most common post-translational modifications. The phosphorylation of the kinase-inducible domain (KID), which is an intrinsically disordered protein (IDP), promotes the folding of KID and binding with the KID-interacting domain (KIX). However, the regulation mechanism of the phosphorylation on KID is still elusive. In this study, the structural ensembles and binding process of pKID and KIX are studied by all-atom enhanced sampling technologies. The results show that more hydrophobic interactions are formed in pKID, which promote the formation of the special hydrophobic residue cluster (HRC). The pre-formed HRC promotes binding to the correct sites of KIX and further lead the folding of pKID. Consequently, a flexible conformational selection model is proposed to describe the binding and folding process of intrinsically disordered proteins. The binding mechanism revealed in this work provides new insights into the dynamic interactions and phosphorylation regulation of proteins.


2012 ◽  
Vol 102 (3) ◽  
pp. 634a-635a
Author(s):  
Hsueh-Liang Chu ◽  
Tsai-Mu Cheng ◽  
Hsing-Yuan Li ◽  
Chia-Ching Chang

2015 ◽  
Vol 11 (7) ◽  
pp. 1850-1856 ◽  
Author(s):  
L. Michel Espinoza-Fonseca ◽  
Ameeta Kelekar

Microsecond molecular dynamics simulations reveal structural and functional features of Noxa, an intrinsically disordered protein, at atomic-level resolution.


2016 ◽  
Vol 25 (8) ◽  
pp. 1420-1429 ◽  
Author(s):  
Ryan C. Killoran ◽  
Modupeola A. Sowole ◽  
Mohammad A. Halim ◽  
Lars Konermann ◽  
Wing-Yiu Choy

2016 ◽  
Vol 52 (39) ◽  
pp. 6541-6544 ◽  
Author(s):  
Pablo Mateos-Gil ◽  
Achilleas Tsortos ◽  
Marisela Vélez ◽  
Electra Gizeli

Characterization of structural changes in an intrinsically disordered protein attached on a QCM-D, with a sensitivity of 1.8 nm or better.


Sign in / Sign up

Export Citation Format

Share Document