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Archak S, Nagaraju J. 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. 2014;10(2):63-7doi: 10.6026/97320630010063.
Archak, S., & 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), 63-7. https://doi.org/10.6026/97320630010063
Archak, Sunil, and Nagaraju, Javaregowda. "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 vol. 10,2 (2014): 63-7. doi: https://doi.org/10.6026/97320630010063
Archak S, Nagaraju J. 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. 2014 Feb 19;10(2):63-7. doi: 10.6026/97320630010063. eCollection 2014. PMID: 24616556; PMCID: PMC3937577.
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Bioinformation. 2014 Feb 19;10(2):63-7. doi: 10.6026/97320630010063. eCollection 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

Sunil Archak, Javaregowda Nagaraju

Affiliations

  1. Division of Genomic Resources, National Bureau of Plant Genetic Resources, Pusa Campus, New Delhi INDIA.
  2. Laboratory of Molecular Genetics, Centre for DNA Fingerprinting and Diagnostics, Hyderabad INDIA.

PMID: 24616556 PMCID: PMC3937577 DOI: 10.6026/97320630010063

Abstract

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.

Keywords: ab initio structure prediction; function prediction; repeat proteins; surface mapping; taxa-specific

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