Deduced sequences show multiple repeats in two D proteins from the tubular accessory glands of Tenebrio molitor
1992
Paesen, G.C. | Weyda, F. | Happ, G.M.
The D group proteins are major secretory products of the tubular accessory glands of male mealworm beetles (Tenebrio molitor). They vary in apparent molecular mass between 22 and 30 kDa. In this paper we present the deduced amino acid sequence of two similar acidic D proteins, termed D1 and D2. These proteins have a structure based on peculiarly repeated sequences. Both molecules consist of three domains. Proceeding from the amino terminus, the acidic A and A' domains are predicted to contain long alpha helical segments. The carboxy-terminal region or B domain is basic and is composed of shorter alpha helical stretches interrupted by turns. D1 and D2 differ in the number of repeats within the A and B domains.
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