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Archak, S. and Nagaraju, J. (2014) Computational analyses of protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) indicate lectin like Ca(2+) binding properties for Eicosapenta Peptide Repeats (EPRs). Bioinformation, 10 (2). pp. 63-67. ISSN 0973-2063

Bioinformation 10 p63 2014 non_sci.pdf - Published Version

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Eicosapenta peptide repeats (EPRs) occur exclusively in flowering plant genomes and exhibit very high amino acid residue conservation across occurrence. DNA and amino acid sequence searches yielded no indications about the function due to absence of similarity to known sequences. Tertiary structure of an EPR protein coded by rice (Oryza sativa japonica) cDNA (GI: 32984786) was determined based on ab initio methodology in order to draw clues on functional significance of EPRs. The resultant structure comprised of seven α-helices and thirteen anti-parallel β-sheets. Surface-mapping of conserved residues onto the structure deduced that (i) regions equivalent to β α4- the primary function of EPR protein could be Ca(2+) binding, and (iii) the putative EPR Ca(2+) binding domain is structurally similar to calcium-binding domains of plant lectins. Additionally, the phylogenetic analysis showed an evolving taxa-specific distribution of EPR proteins observed in some GNA-like lectins.

Item Type: Article
Additional Information: Acknowledgement: Javaregowda Nagaraju passed away on 31 December 2012 and this article is dedicated to his memory
Subjects: Computational Biology
Molecular Biology
Depositing User: Dr P Divakar
Date Deposited: 18 May 2015 18:23
Last Modified: 24 Nov 2015 19:53
URI: http://cdfd.sciencecentral.in/id/eprint/58

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