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.
Pham
Daphne Q-D
DQ
Department of Biological Sciences, Biomedical Research Institute, University of Wisconsin-Parkside, Kenosha 53141-2000, USA. pham@uwp.edu
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
D019476:Insect Proteins; D005293:Ferritins