A possible structural model of members of the CPF family of cuticular proteins implicating binding to components other than chitin

作者：Papandreou Nikos C; Iconomidou Vassiliki A; Willis Judith H; Hamodrakas Stavros J^*

来源：Journal of Insect Physiology, 2010, 56(10): 1420-1426.

DOI：10.1016/j.jinsphys.2010.04.002

• Cuticular proteins structural model
• Lipocalins
• Eight-stranded up and down antiparallel
• beta-pleated sheet barrel
• Insect sex pheromones
• Cuticular lipids

The physical properties of cuticle are determined by the structure of its two major components, cuticular proteins (CPs) and chain, and, also, by their interactions.
A common consensus region (extended R&R Consensus) found in the majority of cuticular proteins, the CPRs, binds to chitin Previous work established that beta-pleated sheet predominates in the Consensus region and we proposed that it is responsible for the formation of helicoldal cuticle Remote sequence similarity between CPRs and a lipocalin, bovine plasma retinal binding protein (RBP), led us to suggest an antiparallel beta-sheet half-barrel structure as the basic folding motif of the R&R Consensus There are several other families of cuticular proteins One of the best defined is CPF. Its four members in Anopheles gat-Tibiae are expressed during the early stages of either pharate pupal or pharate adult development, suggesting that the proteins contribute to the outer regions of the cuticle, the epi- and/or exo-cuticle These proteins did not bind to chitin in the same assay used successfully for CPRs Although CPFs are distinct in sequence from CPRs, the same lipocalin could also be used to derive homology models for one A gambiae and one Drosophila melanogaster CPF. For the CPFs, the basic folding motif predicted is an eight-stranded, antiparallel beta-sheet, full-barrel structure. P

• 出版日期2010-10