Anion-pi interactions in active centers of superoxide dismutases
Samo za registrovane korisnike
2018
Članak u časopisu (Objavljena verzija)

Metapodaci
Prikaz svih podataka o dokumentuApstrakt
We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predic...ted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins.
Ključne reči:
Anion-pi interactions / Superoxide dismutase / Proteins / Active centers / Interaction energyIzvor:
International Journal of Biological Macromolecules, 2018, 106, 559-568Izdavač:
- Elsevier
Finansiranje / projekti:
- Proučavanje fizičkohemijskih i biohemijskih procesa u životnoj sredini koji utiču na zagađenje i istraživanje mogućnosti za minimiziranje posledica (RS-172001)
- Interakcije prirodnih proizvoda, njihovih derivata i kompleksnih jedinjenja sa proteinima i nukleinskim kiselinama (RS-172055)
Napomena:
- The peer-reviewed version: http://cer.ihtm.bg.ac.rs/handle/123456789/3140
DOI: 10.1016/j.ijbiomac.2017.08.050
ISSN: 0141-8130
PubMed: 28811207
WoS: 000417661600063
Scopus: 2-s2.0-85028012582
Institucija/grupa
IHTMTY - JOUR AU - Ribić, Vesna AU - Stojanović, Srđan AU - Zlatović, Mario PY - 2018 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2457 AB - We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predicted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins. PB - Elsevier T2 - International Journal of Biological Macromolecules T1 - Anion-pi interactions in active centers of superoxide dismutases VL - 106 SP - 559 EP - 568 DO - 10.1016/j.ijbiomac.2017.08.050 ER -
@article{ author = "Ribić, Vesna and Stojanović, Srđan and Zlatović, Mario", year = "2018", abstract = "We investigated 1060 possible anion-pi interactions in a data set of 41 superoxide dismutase active centers. Our observations indicate that majority of the aromatic residues are capable to form anion-pi interactions, mainly by long-range contacts, and that there is preference of Trp over other aromatic residues in these interactions. Furthermore, 68% of total predicted interactions in the dataset are multiple anion-pi interactions. Anion-pi interactions are distance and orientation dependent. We analyzed the energy contribution resulting from anion-pi interactions using ab initio calculations. The results showed that, while most of their interaction energies lay in the range from -0 to -4 kcal mol(-1), those energies can be up to -9 kcal mol(-1) and about 34% of interactions were found to be repulsive. Majority of the suggested anion-pi interacting residues in ternary complexes are metal-assisted. Stabilization centers for these proteins showed that all the six residues found in predicted anion-pi interactions are important in locating one or more of such centers. The anion-pi interacting residues in these proteins were found to be highly conserved. We hope that these studies might contribute useful information regarding structural stability and its interaction in future designs of novel metalloproteins.", publisher = "Elsevier", journal = "International Journal of Biological Macromolecules", title = "Anion-pi interactions in active centers of superoxide dismutases", volume = "106", pages = "559-568", doi = "10.1016/j.ijbiomac.2017.08.050" }
Ribić, V., Stojanović, S.,& Zlatović, M.. (2018). Anion-pi interactions in active centers of superoxide dismutases. in International Journal of Biological Macromolecules Elsevier., 106, 559-568. https://doi.org/10.1016/j.ijbiomac.2017.08.050
Ribić V, Stojanović S, Zlatović M. Anion-pi interactions in active centers of superoxide dismutases. in International Journal of Biological Macromolecules. 2018;106:559-568. doi:10.1016/j.ijbiomac.2017.08.050 .
Ribić, Vesna, Stojanović, Srđan, Zlatović, Mario, "Anion-pi interactions in active centers of superoxide dismutases" in International Journal of Biological Macromolecules, 106 (2018):559-568, https://doi.org/10.1016/j.ijbiomac.2017.08.050 . .