Title: Insights into structural features determining odorant affinities to honey bee odorant binding protein 14
Language: English
Authors: Schwaighofer, Andreas  
Pechlaner, Maria 
Oostenbrink, Chris 
Kotlowski, Caroline 
Araman, Can
Mastrogiacomo, Rosa 
Pelosi, Paolo 
Knoll, Wolfgang
Nowak, Christoph
Larisika, Melanie 
Category: Short/Brief/Rapid Communication
Issue Date: 2014
Journal: Biochemical and Biophysical Research Communications
ISSN: 0006-291X
Molecular interactions between odorants and odorant binding proteins (OBPs) are of major importance for understanding the principles of selectivity of OBPs towards the wide range of semiochemicals. It is largely unknown on a structural basis, how an OBP binds and discriminates between odorant molecules. Here we examine this aspect in greater detail by comparing the C-minus OBP14 of the honey bee (Apis mellifera L.) to a mutant form of the protein that comprises the third disulfide bond lacking in C-minus OBPs. Affinities of structurally analogous odorants featuring an aromatic phenol group with different side chains were assessed based on changes of the thermal stability of the protein upon odorant binding monitored by circular dichroism spectroscopy. Our results indicate a tendency that odorants show higher affinity to the wild-type OBP suggesting that the introduced rigidity in the mutant protein has a negative effect on odorant binding. Furthermore, we show that OBP14 stability is very sensitive to the position and type of functional groups in the odorant.
Keywords: Odorant binding protein; circular dichroism; thermal stability; ligand binding; molecular dynamics
DOI: 10.1016/j.bbrc.2014.03.054
Library ID: AC15520860
URN: urn:nbn:at:at-ubtuw:3-7594
Organisation: E164 - Institut für Chemische Technologien und Analytik 
Publication Type: Article
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