Molecular biophysical characterization of the third FF domain of Homo sapiens Prp40 homolog A
| Autor: | Belinda Pastrana-Rios, Adalberto Díaz Casas, Odalys Sánchez Negrón, Andrea P. Caro Muñiz, Ana R. Cebollero López, Stewart R. Malavé Ramos, Gabriela Casanova Sepúlveda |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Circular dichroism Organic Chemistry Peptide Isothermal titration calorimetry 010402 general chemistry 01 natural sciences 0104 chemical sciences Analytical Chemistry Inorganic Chemistry 03 medical and health sciences 030104 developmental biology chemistry Homo sapiens RNA splicing Centrin Biophysics Nuclear protein Two-dimensional nuclear magnetic resonance spectroscopy Spectroscopy |
| Zdroj: | Journal of Molecular Structure. 1167:174-179 |
| ISSN: | 0022-2860 |
| DOI: | 10.1016/j.molstruc.2018.04.059 |
| Popis: | Homo sapiens Prp40 Homolog A ( Hs Prp40A) is a nuclear protein that is involved in pre-mRNA splicing. This modular protein has two WW domains followed by six tandem FF domains. Previous studies demonstrate that the WW domain-mediated interactions of Hs Prp40A are implicated in genetic disorders such as Huntington's disease and Rett syndrome. However, little is known about the biological implications related to Hs Prp40A's FF domains. Recently, we determined that Hs Prp40A peptide interacts with high affinity with a calcium-binding protein known as centrin using isothermal titration calorimetry and two-dimensional infrared correlation spectroscopy. Interestingly, this centrin-binding site is located within the third FF (FF 3 ) domain of Hs Prp40A. Herein, we present a comparative molecular biophysical study using circular dichroism and two-dimensional infrared correlation spectroscopy to explore the molecular behavior of Hs Prp40A's FF 3 domain under thermal stress. These results may provide new insights about the stability of Hs Prp40A's FF 3 domain. |
| Databáze: | OpenAIRE |
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