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In Silico Pharmaco-Gene-Informatic Identification of Insulin-Like Proteins in Plants
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Author(s): Koona Saradha Jyothi (Andhra University, India), G. R. Sridhar (Endocrine and Diabetes Centre, India), Kudipudi Srinivas (V R Siddhartha Engineering College, India), B. Subba Rao (Andhra University, India)and Allam Apparao (Jawaharlal Nehru Technological University, India)
Copyright: 2013
Pages: 16
Source title:
Bioinformatics: Concepts, Methodologies, Tools, and Applications
Source Author(s)/Editor(s): Information Resources Management Association (USA)
DOI: 10.4018/978-1-4666-3604-0.ch051
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Abstract
This chapter presents an extension of the authors’ earlier work, where they showed that nucleotide/amino acid sequences related to insulin occurred in the plant kingdom. It was believed that plants did not have, nor did they need insulin, a protein hormone considered to be restricted to the animal kingdom. In the current study, the human insulin sequence was initially obtained from UniProt/SwissProt (accession no. P01308). Plant genome sequences were obtained from NCBI PubMed (Bauhinia purpurea [Gi|229412], Vigna unguiculata [P83770], and Canavalia ensiformis [Gi|7438602]. Scores were obtained from ProtFun 2.2 [http://www.cbs.dtu.dk/services/ProtFun/]. At the next stage, functions of insulin and glucokinin (insulin like proteins in plants) were predicted by the Protein Function Prediction database (http://dragon.bio.purdue.edu/pfp/index.html), followed by functional site prediction from the ELM database (http://elm.eu.org/). ProtFun predicted the following functions: human insulin (Cell envelope), Jack bean (Energy metabolism), Bauhinia purpurea(Translation). The amino acid Glycine at 32 positions was most highly conserved. Present predictions advocate the use of these sequences (QHLCGS motif) as targets for probing the other plants with lesser homology. In summary our in silico studies have suggested that Bauhinia purpurea (Purple orchid tree-BP), Vigna unguiculata (Cow pea-CP) and Canavalia ensiformis (Jack bean-JB) have conserved the important regions of the human insulin protein.
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