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Structural and Functional Characterization of Arabidopsis thaliana WW Domain Containing Protein F4JC80

  • Amit Das
  • Simanti Bhattacharya
  • Angshuman Bagchi
  • Rakhi Dasgupta
Chapter
Part of the SpringerBriefs in Applied Sciences and Technology book series (BRIEFSAPPLSCIENCES)

Abstract

WW domains are the smallest known independently foldable protein structural motifs that are involved in cellular events like protein turnover, splicing, development, and tumor growth control. These motifs bind the polyproline rich ligands. While the WW domains of animal origin are well characterized, the same from plant origin are not well documented yet. Despite the small repertoire of WW proteome of plants (in comparison to animal WW proteome) functional diversity is reported to be equally vivid for plants also. Here, for the first time, we report the structural and functional properties of an Arabidopsis thaliana (At) WW domain containing protein F4JC80 by using homology modeling and docking techniques. Our findings report that the At F4JC80 protein contains two WW domains which bear the standard triple β sheet structure and structurally and functionally resemble Class I WW domains of E3 ubiquitin ligase family but their structural differences impact their polypeptide binding abilities differently.

Keywords

WW domain Arabidopsis thaliana Transcription Splicing Homology modeling Molecular docking 

Notes

Acknowledgments

The authors would like to thank the members of RD and AB laboratory for their continuous support and critical assessments. AD and SB would like to thank CSIR (India) and UGC (India), respectively, for their Ph.D. fellowships.

Author Contributions AD and SB have performed the modeling and docking studies and drafted the manuscript. RD and AB have analyzed the results and prepared the final version of the manuscript. All the authors have read and approved the final version of the manuscript.

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Copyright information

© The Author(s) 2015

Authors and Affiliations

  1. 1.Department of Biochemistry and BiophysicsUniversity of KalyaniKalyani, NadiaIndia

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