Fig. 2 | Scientific Data

Fig. 2

From: iOBPdb A Database for Experimentally Determined Functional Characterization of Insect Odorant Binding Proteins

Fig. 2The alternative text for this image may have been generated using AI.

The functional domains of OBPs and their structures. The structural depiction of a classical OBP is with six alpha helices (denoted in black as α1- α6) and is held in place by three disulfide bonds (shown in red). The alpha helices are linked by short sequences with no canonical structure (shown in blue). The signaling peptide (represented as SP in yellow) at the start of the sequence marks the protein for excretion by the cell and is cleaved before entering the extracellular environment. Different arrangements of OBPs differ regarding the number of amino acids (AAs), the number of cysteine bonds, and the number of alpha helices. Note that due to the immense diversity of OBPs, many OBPs may exhibit conformations not shown in this figure.

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