prikaz prve stranice dokumenta Conservation of the conformational dynamics and ligand binding within M49 enzyme family
  Download
PDF 1.76 MB
Scientific paper - Original scientific paper
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.

Cite this document

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, no. 24, pp. 13310-13322. https://doi.org/10.1039/c7ra13059g

Kazazić, S., Z. Karačić, I. Sabljić, Dejan Agić, M. Tomin, M. Abramović, M. Dadlez, A. Tomić and S. Tomić. "Conservation of the conformational dynamics and ligand binding within M49 enzyme family." RSC ADVANCES 8, no. 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), pp. 13310-13322. doi: 10.1039/c7ra13059g

Kazazić S, Karačić Z, Sabljić I, Agić D, Tomin M, Abramović M, and sur.. Conservation of the conformational dynamics and ligand binding within M49 enzyme family. RSC ADVANCES [Internet]. [cited 2024 December 30];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, no. 24, pp. 13310-13322. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:151:531240. [Accessed: 30 December 2024]

Please login to the repository to save this object to your list.
Metadata
Title (english)Conservation of the conformational dynamics and ligand binding within M49 enzyme family
AuthorS. Kazazić
AuthorZ. Karačić
AuthorI. Sabljić
AuthorDejan Agić
AuthorM. Tomin
AuthorM. Abramović
AuthorM. Dadlez
AuthorA. Tomić
AuthorS. Tomić
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)
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
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - domestic
Publication versionPublished version
Journal titleRSC ADVANCES
Numberingvol. 8, no. 24, pp. 13310-13322
e-ISSN2046-2069
DOIhttps://doi.org/10.1039/c7ra13059g
URN:NBNurn:nbn:hr:151:531240
Accepted2018-03-28
Document URLhttps://pubs.rsc.org/en/content/articlepdf/2018/ra/c7ra13059g
Type of resourceText
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2024-06-18 08:57:47