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izvor podataka: crosbi

Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III (CROSBI ID 254784)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Agić, Dejan ; Brkić, Hrvoje ; Kazazić, Saša ; Tomić, Antonija ; Abramić, Marija Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III // Journal of biomolecular structure & dynamics, 37 (2019), 14; 3596-3606. doi: 10.1080/07391102.2018.1521343

Podaci o odgovornosti

Agić, Dejan ; Brkić, Hrvoje ; Kazazić, Saša ; Tomić, Antonija ; Abramić, Marija

engleski

Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III

Human dipeptidyl peptidase III (hDPP III) is a zinc-exopeptidase of the family M49 involved in final steps of intracellular protein degradation and in cytoprotective pathway Keap1-Nrf2. Biochemical and structural properties of this enzyme have been extensively investigated, but the knowledge on its contacts with other proteins is scarce. Previously, polypeptide aprotinin was shown to be a competitive inhibitor of hDPP III hydrolytic activity. In the present study, aprotinin was first investigated as a potential substrate of hDPP III, but no degradation products were demonstrated by MALDI-TOF mass spectrometry. Subsequently, molecular details of the protein- protein interaction between aprotinin and hDPP III were studied by molecular modeling. Docking and long molecular dynamics (MD) simulations have shown that aprotinin interacts by its canonical binding epitope with the substrate binding cleft of hDPP III. Thereby, free N-terminus of aprotinin is distant from the active-site zinc. Enzyme- inhibitor complex is stabilized by intermolecular hydrogen bonding network, electrostatic and hydrophobic interactions which mostly involve constituent amino acid residues of the hDPP III substrate binding subsites S1, S1', S2, S2' and S3'. This is the first study that gives insight into aprotinin binding to an metallopeptidase

aprotinin ; BPTI ; dipeptidyl peptidase III ; metallopeptidase ; MD simulation

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Podaci o izdanju

37 (14)

2019.

3596-3606

objavljeno

0739-1102

1538-0254

10.1080/07391102.2018.1521343

Povezanost rada

Biologija, Fizika, Kemija

Poveznice
Indeksiranost