Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	Influence of pH on indole-dependent heterodimeric interactions between Anopheles gambiae odorant-binding proteins OBP1 and OBP4
Δημιουργός/Συγγραφέας:	Mam, Bhavika Tsitsanou, Katerina E Liggri, Panagiota G V Saitta, Francesca Stamati, Evgenia C V Mahita, Jarjapu Leonis, Georgios Drakou, Christina E [EL] Παπαδόπουλος, Μάνθος Γ.[EN] Papadopoulos, Manthos G. Arnaud, Philippe Offmann, Bernard Fessas, Dimitrios Sowdhamini, Ramanathan [EL] Ζωγράφος, Σπύρος Ε.[EN] Zographos, Spyros E.
Εκδότης:	International Journal of Biological Macromolecules
Ημερομηνία:	2023-06-16
Γλώσσα:	Αγγλικά
ISSN:	01418130
DOI:	10.1016/j.ijbiomac.2023.125422
Άλλο:	37330089
Περίληψη:	Insect Odorant Binding Proteins (OBPs) constitute important components of their olfactory apparatus, as they are essential for odor recognition. OBPs undergo conformational changes upon pH change, altering their interactions with odorants. Moreover, they can form heterodimers with novel binding characteristics. Anopheles gambiae OBP1 and OBP4 were found capable of forming heterodimers possibly involved in the specific perception of the attractant indole. In order to understand how these OBPs interact in the presence of indole and to investigate the likelihood of a pH-dependent heterodimerization mechanism, the crystal structures of OBP4 at pH 4.6 and 8.5 were determined. Structural comparison to each other and with the OBP4-indole complex (3Q8I, pH 6.85) revealed a flexible N-terminus and conformational changes in the α4-loop-α5 region at acidic pH. Fluorescence competition assays showed a weak binding of indole to OBP4 that becomes further impaired at acidic pH. Additional Molecular Dynamic and Differential Scanning Calorimetry studies displayed that the influence of pH on OBP4 stability is significant compared to the modest effect of indole. Furthermore, OBP1-OBP4 heterodimeric models were generated at pH 4.5, 6.5, and 8.5, and compared concerning their interface energy and cross-correlated motions in the absence and presence of indole. The results indicate that the increase in pH may induce the stabilization of OBP4 by increasing its helicity, thereby enabling indole binding at neutral pH that further stabilizes the protein and possibly promotes the creation of a binding site for OBP1. A decrease in interface stability and loss of correlated motions upon transition to acidic pH may provoke the heterodimeric dissociation allowing indole release. Finally, we propose a potential OBP1-OBP4 heterodimer formation/disruption mechanism induced by pH change and indole binding.
Τίτλος πηγής δημοσίευσης:	International journal of biological macromolecules
Τόμος/Κεφάλαιο:	245
Θεματική Κατηγορία:	[EL] Δομική Βιολογία[EN] Structural Biology [EL] Βιοχημεία[EN] Biochemistry [EL] Χημική Βιολογία[EN] Chemical Biology
Λέξεις-Κλειδιά:	Heterodimer Indole Insect olfaction Interface energetics Molecular dynamics Mosquito OBP Odorant binding protein Structure pH-dependence Animals Odorants Binding Sites Indoles Hydrogen-Ion Concentration Insect Proteins Anopheles Receptors, Odorant
Ηλεκτρονική διεύθυνση στον εκδότη (link):	https://doi.org/10.1016/j.ijbiomac.2023.125422
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο