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Conservation of the conformational dynamics and ligand binding within M49 enzyme family
RSC ADVANCES, 8 (2018), 24; 13310-13322. https://doi.org/10.1039/c7ra13059g
Kazazić, S.; Karačić, Z.; Sabljić, I.; Agić, Dejan; Tomin, M.; Abramović, M.; Dadlez, M.; Tomić, A.; Tomić, S.

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Kazazić, S., Karačić, Z., Sabljić, I., Agić, D., Tomin, M., Abramović, M. ... Tomić, S.. Conservation of the conformational dynamics and ligand binding within M49 enzyme family. RSC ADVANCES, 8. (24), 13310-13322. doi: 10.1039/c7ra13059g

Kazazić, S., et al. "Conservation of the conformational dynamics and ligand binding within M49 enzyme family." RSC ADVANCES, vol. 8, br. 24, str. 13310-13322. https://doi.org/10.1039/c7ra13059g

Kazazić, S., Z. Karačić, I. Sabljić, Dejan Agić, M. Tomin, M. Abramović, M. Dadlez, A. Tomić i S. Tomić. "Conservation of the conformational dynamics and ligand binding within M49 enzyme family." RSC ADVANCES 8, br. 24 13310-13322. https://doi.org/10.1039/c7ra13059g

Kazazić, S., et al. 'Conservation of the conformational dynamics and ligand binding within M49 enzyme family', RSC ADVANCES, 8(24), str. 13310-13322. doi: 10.1039/c7ra13059g

Kazazić S, Karačić Z, Sabljić I, Agić D, Tomin M, Abramović M, i sur.. Conservation of the conformational dynamics and ligand binding within M49 enzyme family. RSC ADVANCES [Internet]. [pristupljeno 12.07.2024.];8(24):13310-13322. doi: 10.1039/c7ra13059g

S. Kazazić, et al., "Conservation of the conformational dynamics and ligand binding within M49 enzyme family", RSC ADVANCES, vol. 8, br. 24, str. 13310-13322. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:151:531240. [Citirano: 12.07.2024.]

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Naslov (engleski)Conservation of the conformational dynamics and ligand binding within M49 enzyme family
AutorS. Kazazić
AutorZ. Karačić
AutorI. Sabljić
AutorDejan Agić
AutorM. Tomin
AutorM. Abramović
AutorM. Dadlez
AutorA. Tomić
AutorS. Tomić
Autorova ustanovaSveučilište Josipa Jurja Strossmayera u Osijeku
Fakultet agrobiotehničkih znanosti Osijek
(Zavod za agroekologiju i zaštitu okoliša)
Znanstveno / umjetničko
područje, polje i grana		BIOTEHNIČKE ZNANOSTI
Poljoprivreda (agronomija)
Agrokemija
Sažetak (engleski)
The hydrogen deuterium exchange (HDX) mass spectrometry combined with molecular dynamics (MD) simulations was employed to investigate conformational dynamics and ligand binding within the M49 family (dipeptidyl peptidase III family). Six dipeptidyl peptidase III (DPP III) orthologues, human, yeast, three bacterial and one plant (moss) were studied. According to the results, all orthologues seem to be quite compact wherein DPP III from the thermophile Caldithrix abyssi seems to be the most compact. The protected regions are located within the two domains core and the overall flexibility profile consistent with semi-closed conformation as the dominant protein form in solution. Besides conservation of conformational dynamics within the M49 family, we also investigated the ligand, pentapeptide tynorphin, binding. By comparing HDX data obtained for unliganded protein with those obtained for its complex with tynorphin it was found that the ligand binding mode is conserved within the family. Tynorphin binds within inter-domain cleft, close to the lower domain b-core and induces its stabilization in all orthologues. Docking combined with MD simulations revealed details of the protein flexibility as well as of the enzyme–ligand interactions
Ključne riječi (engleski)
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran - domaća recenzija
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaRSC ADVANCES
Brojčani podacivol. 8, br. 24, str. 13310-13322
e-ISSN2046-2069
DOIhttps://doi.org/10.1039/c7ra13059g
URN:NBNurn:nbn:hr:151:531240
Datum prihvaćanja za tisak2018-03-28
URL dokumentahttps://pubs.rsc.org/en/content/articlepdf/2018/ra/c7ra13059g
Vrsta resursaTekst
Prava pristupaOtvoreni pristup
Uvjeti korištenjaIkona licence Zaštićeno autorskim pravom.
Datum i vrijeme pohrane2024-06-18 08:57:47