Structural Analyses of the Mode of Binding Between AANAT Protein with 14-3-3 Protein Involved in Human Melatonin Synthesis

  • Ananya Ali
  • Sanchari Bhattacharjee
  • Angshuman Bagchi
Conference paper
Part of the Advances in Intelligent Systems and Computing book series (AISC, volume 340)


Arylalkylamine N-acetyltransferase (AANAT) or Serotonin N-acetyltransferase is one of the key enzymes for the synthesis of melatonin in humans. In the process, the regular binding partner of this AANAT protein is 14-3-3 protein. A mutation of A129T in the AANAT protein leads to decreased functionality of the AANAT protein. So far the mechanistic details of this loss of binding have not been elucidated. In the present work, we tried to utilize structural bioinformatic approach to understand the differences in pattern of bindings between AANAT wild type and mutant forms. We used molecular mechanics calculations to describe the interactions of wild type and mutant AANAT proteins with its binding partner 14-3-3 proteins. So far, this is the first report that characterizes the difference in binding between the two forms of the protein. Therefore, the results from this study may be useful for the development of drugs in patients having impaired melatonin synthesis.


Protein-protein interaction Arylalkylamine N-acetyltransferase Molecular modeling Molecular mechanics Mutations 



The authors would like to thank the DST-PURSE program 2012-2015 going on in the Department of Biochemistry and Biophysics, University of Kalyani for providing different instrumental and infrastructural support. The authors are also thankful to the DBT sponsored Bioinformatics Infrastructure Facility in the Department of Bio-chemistry and Biophysics, University of Kalyani for the necessary support.


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Copyright information

© Springer India 2015

Authors and Affiliations

  • Ananya Ali
    • 1
  • Sanchari Bhattacharjee
    • 1
  • Angshuman Bagchi
    • 1
  1. 1.Department of Biochemistry and BiophysicsUniversity of KalyaniKalyani, NadiaIndia

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