title: Molecular modeling of insect ferritins.
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 alpha-helices were located in the Dipteran and Lepidopteran, but not in Homopteran ferritin subunits.
authors.affiliation: Department of Biological Sciences, Biomedical Research Institute, University of Wisconsin-Parkside, Kenosha 53141-2000, USA. pham@uwp.edu
authors.forename: Daphne Q-D
authors.initials: DQ
authors.lastname: Pham
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005293:Ferritins / Q000737:chemistry* / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid; D014714:Vertebrates
chemical_list: D019476:Insect Proteins; D005293:Ferritins