Affiliations: Department of Biological Sciences, Biomedical Research
Institute, University of Wisconsin-Parkside, Kenosha, WI 53141-2000, USA;
[email protected]
Abstract: 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 á-helices were located in the Dipteran and Lepidopteran,
but not in Homopteran ferritin subunits.
