Spider mites are one of the major agricultural pests, feeding on a large variety of plants. As a contribution to understanding chemical communication in these arthropods, we have characterized a recently discovered class of odorant-binding proteins (OBPs) in . As in other species of Chelicerata, the four OBPs of contain six conserved cysteines paired in a pattern (C1-C6, C2-C3, C4-C5) differing from that of insect counterparts (C1-C3, C2-C5, C4-C6). Proteomic analysis uncovered a second family of OBPs, including twelve members that are likely to be unique to . A three-dimensional model of TurtOBP1, built on the recent X-ray structure of OBP1, shows protein folding different from that of insect OBPs, although with some common features. Ligand-binding experiments indicated some affinity to coniferyl aldehyde, but specific ligands may still need to be found among very large molecules, as suggested by the size of the binding pocket.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8269058 | PMC |
http://dx.doi.org/10.3390/ijms22136828 | DOI Listing |
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