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HSP90 interaction with other proteins and cofactors

Grant number: 17/01074-9
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): June 01, 2017
Effective date (End): July 31, 2018
Field of knowledge:Biological Sciences - Biochemistry - Chemistry of Macromolecules
Principal Investigator:Carlos Henrique Inacio Ramos
Grantee:Glaucia Melina Squizato Pinheiro de Castro
Home Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Associated research grant:12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis, AP.TEM

Abstract

The great importance of understanding the interaction of HSP90 with other proteins can be verified by the fact that this chaperone works as a 'hub' for it interacts with at least 10% of the proteins expressed in eukaryotes. However, little information exists about the regions of interaction and how other factors affect this interaction. The high molecular mass of Hsp90, the interactions being transient and the difficulty of obtaining proteins in high concentration are difficult tasks that need to be addressed in order to increase our understandif of the HSP90 netwirk. In addition to the above, there is little information about how other factors besides interaction with proteins affect the structure and function of HSP90. To obtain information related to the above topics, we will use molecular biophysics and structural biology tools to investigate the regions of interaction between HSP90 and co-chaperones with other proteins and also measure the effect of cofactors (nucleotides, metals, peptides, etc.). The large-scale study of the effect of these cofactors on proteins has gained much relevance recently and its application in chaperones cannot be ignored. (AU)

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
PINHEIRO, GLAUCIA M. S.; AMORIM, GISELE C.; IQBAL, ANWAR; ALMEIDA, FABIO C. L.; RAMOSA, C. H. I. Solution NMR investigation on the structure and function of the isolated J-domain from Sis1: Evidence of transient inter-domain interactions in the full-length protein. Archives of Biochemistry and Biophysics, v. 669, p. 71-79, JUL 15 2019. Web of Science Citations: 1.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.