Molecular modeling of insect ferritins.
Amino acid sequences of ferritin subunits from three orders of insects (Diptera: Drosophila and Aedes; Lepidoptera: Calpodes and Manduca; and Homoptera: Nilaparvata) were obtained from the public database, and analyzed using structural modeling algorithms. Pattern recognition analysis identifies cell attachment, glycosylation, myristoylation, microbody targeting, phosphorylation, cAMP/cGMP dependent, protein kinase C, casein kinase, and tyrosine kinase sites in these subunits. The modeling analyses suggest that the insect heavy-chain homologues are similar to their vertebrate analogues and retain all active sites, including the ferroxidase center. On the contrary, the insect light-chain homologues are different from their vertebrate counterparts, and show none of these features. Five alpha-helices were located in the Dipteran and Lepidopteran, but not in Homopteran ferritin subunits.[1]References
- Molecular modeling of insect ferritins. Pham, D.Q. In Silico Biol. (Gedrukt) (2002) [Pubmed]
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