prikaz prve stranice dokumenta Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III
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Scientific paper - Original scientific paper
Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III
JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS, 37 (2018), 14; 3556-3606. https://doi.org/10.1080/07391102.2018.1521343
Agić, Dejan; Brkić, H.; Kazazić, S.; Tomić, A.; Abramović, M.

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Agić, D., Brkić, H., Kazazić, S., Tomić, A. & Abramović, M.. Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III. JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS, 37. (14), 3556-3606. doi: 10.1080/07391102.2018.1521343

Agić, Dejan, et al. "Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III." JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS, vol. 37, no. 14, pp. 3556-3606. https://doi.org/10.1080/07391102.2018.1521343

Agić, Dejan, H. Brkić, S. Kazazić, A. Tomić and M. Abramović. "Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III." JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS 37, no. 14 3556-3606. https://doi.org/10.1080/07391102.2018.1521343

Agić, D., et al. 'Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III', JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS, 37(14), pp. 3556-3606. doi: 10.1080/07391102.2018.1521343

Agić D, Brkić H, Kazazić S, Tomić A, Abramović M. Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III. JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS [Internet]. [cited 2024 December 22];37(14):3556-3606. doi: 10.1080/07391102.2018.1521343

D. Agić, H. Brkić, S. Kazazić, A. Tomić and M. Abramović, "Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III", JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS, vol. 37, no. 14, pp. 3556-3606. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:151:779701. [Accessed: 22 December 2024]

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Metadata
Title (english)Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III
AuthorDejan Agić
AuthorH. Brkić
AuthorS. Kazazić
AuthorA. Tomić
AuthorM. Abramović
Author's institutionJosip Juraj Strossmayer University of Osijek
Faculty of Agrobiotechnical Sciences Osijek
(Department of agroecology and Enviroment Protection)
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Agronomy
Agrochemistry
Abstract (english)
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 this 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 a metallopeptidase.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - domestic
Publication versionPublished version
Journal titleJOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS
Numberingvol. 37, no. 14, pp. 3556-3606
p-ISSN0739-1102
e-ISSN1538-0254
DOIhttps://doi.org/10.1080/07391102.2018.1521343
URN:NBNurn:nbn:hr:151:779701
Accepted2018-09-03
Document URLhttps://www.tandfonline.com/doi/pdf/10.1080/07391102.2018.1521343?needAccess=true
Type of resourceText
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2024-06-18 08:27:02