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Volume 1

Full article

Molecular modeling of insect ferritins

Daphne Q.-D. Pham

Department of Biological Sciences, Biomedical Research Institute, University of Wisconsin-Parkside, Kenosha, WI 53141-2000, USA.
E-mail: pham@uwp.edu


Edited by E. Wingender; received April 19, 2000; revised July 24, 2000; accepted July 25, 2000

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 -helices were located in the Dipteran and Lepidopteran, but not in Homopteran ferritin subunits.

Key words: Insects, mosquito, heavy-chain, light-chain, ferritin, modeling