Next Article in Journal
Resistance to the Antiproliferative In Vitro Effect of PI3K-Akt-mTOR Inhibition in Primary Human Acute Myeloid Leukemia Cells Is Associated with Altered Cell Metabolism
Next Article in Special Issue
Discovery of Cryoprotective Activity in Human Genome-Derived Intrinsically Disordered Proteins
Previous Article in Journal
Corylin Suppresses Hepatocellular Carcinoma Progression via the Inhibition of Epithelial-Mesenchymal Transition, Mediated by Long Noncoding RNA GAS5
Previous Article in Special Issue
Insights into the Molecular Mechanisms of Alzheimer’s and Parkinson’s Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2018, 19(2), 381; https://doi.org/10.3390/ijms19020381

How Do We Study the Dynamic Structure of Unstructured Proteins: A Case Study on Nopp140 as an Example of a Large, Intrinsically Disordered Protein

1
Department of Chemistry, Kookmin University 77, Jeongneung-Ro, Seongbuk-gu, Seoul 02707, Korea
2
New Drug Development Center, Osong Medical Innovation Foundation, Osong Sengmyung-Ro 123, Osong-eup, Heungdeok-gu, Cheongju-si, Chungbuk 28160, Korea
*
Author to whom correspondence should be addressed.
Received: 4 January 2018 / Revised: 22 January 2018 / Accepted: 23 January 2018 / Published: 27 January 2018
Full-Text   |   PDF [3693 KB, uploaded 27 January 2018]   |  

Abstract

Intrinsically disordered proteins (IDPs) represent approximately 30% of the human genome and play key roles in cell proliferation and cellular signaling by modulating the function of target proteins via protein–protein interactions. In addition, IDPs are involved in various human disorders, such as cancer, neurodegenerative diseases, and amyloidosis. To understand the underlying molecular mechanism of IDPs, it is important to study their structural features during their interactions with target proteins. However, conventional biochemical and biophysical methods for analyzing proteins, such as X-ray crystallography, have difficulty in characterizing the features of IDPs because they lack an ordered three-dimensional structure. Here, we present biochemical and biophysical studies on nucleolar phosphoprotein 140 (Nopp140), which mostly consists of disordered regions, during its interaction with casein kinase 2 (CK2), which plays a central role in cell growth. Surface plasmon resonance and electron paramagnetic resonance studies were performed to characterize the interaction between Nopp140 and CK2. A single-molecule fluorescence resonance energy transfer study revealed conformational change in Nopp140 during its interaction with CK2. These studies on Nopp140 can provide a good model system for understanding the molecular function of IDPs. View Full-Text
Keywords: intrinsically disordered protein (IDP); nucleolar phosphoprotein 140 (Nopp140); conformational study; casein kinase 2 (CK2) intrinsically disordered protein (IDP); nucleolar phosphoprotein 140 (Nopp140); conformational study; casein kinase 2 (CK2)
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Na, J.-H.; Lee, W.-K.; Yu, Y.G. How Do We Study the Dynamic Structure of Unstructured Proteins: A Case Study on Nopp140 as an Example of a Large, Intrinsically Disordered Protein. Int. J. Mol. Sci. 2018, 19, 381.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top