Human DPP III - Keap1 interactions (CROSBI ID 676405)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija
Podaci o odgovornosti
Tomin, Marko ; Tomić, Sanja
engleski
Human DPP III - Keap1 interactions
Kelch-like ECH associated protein 1 (Keap1) is a cellular sensor for oxidative stress and a negative regulator of the nuclear erythroid 2–related factor 2 (Nrf2). A cytosolic metallopeptidase dipeptidyl peptidase III (DPP III) has been shown to interact with the Kelch domain of Keap1 via the ETGE motif located in a flexible loop belonging to the upper domain. Using the previously developed models of the DPP III -Keap1 complex, we are trying to identify the conformation of the ETGE-containing loop in the complex, as well as the work required to achieve the active conformation for Keap1 binding.Although the DPP III -Keap1 interaction through the conserved ETGE motif has been experimentally confirmed [4], the extensive MD simulations of the human DPP suggest that the loop is attached to the upper domain of DPP III at all times. In order to quantify the thermodynamic barrier and the work required for the loop translocation, as well as the subsequent complex formation, we have used steered MD simulations, adaptive steered MD simulations and conventional MD simulations in conjunction with the MM-PBSA energy calculations.
Dipeptidyl peptidase III ; DPP III ; molecular dynamics ; protein-protein interactions
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
Podaci o prilogu
24-24.
2019.
objavljeno
Podaci o matičnoj publikaciji
Computational Chemistry Day 2019 Book of Abstracts
Zagreb: Prirodoslovno-matematički fakultet Sveučilišta u Zagrebu
978-953-6076-51-2
Podaci o skupu
Computational Chemistry Day 2019
poster
11.05.2019-11.05.2019
Zagreb, Hrvatska