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Conservation of the conformational dynamics and ligand binding within M49 enzyme family


Kazazić, Saša; Karačić, Zrinka; Sabljić, Igor; Agić, Dejan; Tomin, Marko; Abramić, Marija; Dadlez, Michal; Tomić, Antonija; Tomić, Sanja
Conservation of the conformational dynamics and ligand binding within M49 enzyme family // RSC Advances, 8 (2018), 24; 13310-13322 doi:10.1039/c7ra13059g (međunarodna recenzija, članak, znanstveni)


Naslov
Conservation of the conformational dynamics and ligand binding within M49 enzyme family

Autori
Kazazić, Saša ; Karačić, Zrinka ; Sabljić, Igor ; Agić, Dejan ; Tomin, Marko ; Abramić, Marija ; Dadlez, Michal ; Tomić, Antonija ; Tomić, Sanja

Izvornik
RSC Advances (2046-2069) 8 (2018), 24; 13310-13322

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Dipeptidyl peptidase III ; DPP III ; hydrogen-deuterium exchange ; HDX ; MD simulations ; conformational dynamics

Sažetak
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 β-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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biotehnologija



POVEZANOST RADA


Projekt / tema
FP7-REGPOT- 2012-2013-1
HRZZ-IP-2013-11-7235 - Povezanost fleksibilnosti, aktivnosti i strukture u porodici dipeptidil-peptidaza III (Sanja Tomić, )

Ustanove
Fakultet agrobiotehničkih znanosti Osijek,
Institut "Ruđer Bošković", Zagreb,
Sveučilište J. J. Strossmayera u Osijeku

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus


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