Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: A comparative perspective
| Autor: | Erika Chang de Azevedo, Vanessa Thomaz Rodrigues Kiraly, Júlio César Borges, Fernando A. Melo, Lisandra M. Gava, Alessandro S. Nascimento, Carlos H.I. Ramos, Karine Minari, Fernanda Aparecida Heleno Batista, Fabio Rogerio de Moraes |
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| Přispěvatelé: | Universidade de São Paulo (USP), Universidade Federal de São Carlos (UFSCar), Universidade Estadual Paulista (Unesp), Universidade Estadual de Campinas (UNICAMP) |
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Protein Conformation Enthalpy Cellular homeostasis Hsp90 Protein-ligand interaction 02 engineering and technology Molecular dynamics Biochemistry law.invention 03 medical and health sciences Adenosine Triphosphate Structural Biology law Humans Nucleotide Amino Acid Sequence HSP90 Heat-Shock Proteins Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences STD-NMR biology Isothermal titration calorimetry General Medicine ITC PROTEÍNAS 021001 nanoscience & nanotechnology Yeast Adenosine Diphosphate chemistry biology.protein Recombinant DNA Thermodynamics 0210 nano-technology Protein Binding |
| Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP Web of Science Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2019.02.116 |
| Popis: | Made available in DSpace on 2019-10-04T12:37:16Z (GMT). No. of bitstreams: 0 Previous issue date: 2019-06-01 Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Hsp90s are key proteins in cellular homeostasis since they interact with many client proteins. Several studies indicated that Hsp9Os are potential targets for treating diseases, such as cancer or malaria. It has been shown that Hsp9Os from different organisms have peculiarities despite their high sequence identity. Therefore, a detailed comparative analysis of several Hsp90 proteins is relevant to the overall understanding of their activity. Accordingly, the goal of this work was to evaluate the interaction of either ADP or ATP with recombinant Hsp9Os from different organisms ( human et and (3 isoforms, Plasmodium falciparum, Leishmania braziliensis, yeast and sugarcane) by isothermal titration calorimetry. The measured thermodynamic signatures of those interactions indicated that despite the high identity among all Hsp90s, they have specific thermodynamic characteristics. Specifically, the interactions with ADP are driven by enthalpy but are opposed by entropy, whereas the interaction with ATP is driven by both enthalpy and entropy. Complimentary structural and molecular dynamics studies suggested that specific interactions with ADP that differ from those with ATP may contribute to the observed enthalpies and entropies. Altogether, the data suggest that selective inhibition may be more easily achieved using analogues of the Hsp90-ADP bound state than those of Hsp90-ATP bound state. (C) 2019 Elsevier B.V. All rights reserved. Univ Sao Paulo, Sao Carlos Inst Chem, BR-13566590 Sao Carlos, SP, Brazil Univ Fed Sao Carlos, Ctr Biol & Hlth Sci, BR-13560970 Sao Carlos, SP, Brazil Univ Sao Paulo, Sao Carlos Inst Phys, BR-13560970 Sao Carlos, SP, Brazil Sao Paulo State Univ, Multiuser Ctr Biol Innovat CMIB, Biosci Languages & Exact Sci Inst, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil Univ Campinas UNICAMP, Inst Chem, BR-13083970 Campinas, SP, Brazil Sao Paulo State Univ, Multiuser Ctr Biol Innovat CMIB, Biosci Languages & Exact Sci Inst, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil FAPESP: 2009/53989-4 FAPESP: 2011/23110-0 FAPESP: 2012/50161-8 FAPESP: 2013/25646-0 FAPESP: 2014/07206-6 FAPESP: 2015/26722-8 FAPESP: 2017/07335-9 FAPESP: 2017/18173-0 CNPq: 471415/2013-8 CNPq: 303129/2015-8 |
| Databáze: | OpenAIRE |
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