Anzeige
Erschienen in:
2015 | OriginalPaper | Buchkapitel
Structural Analyses of the Mode of Binding Between AANAT Protein with 14-3-3 Protein Involved in Human Melatonin Synthesis
verfasst von : Ananya Ali, Sanchari Bhattacharjee, Angshuman Bagchi
Erschienen in: Information Systems Design and Intelligent Applications
Verlag: Springer India
Aktivieren Sie unsere intelligente Suche, um passende Fachinhalte oder Patente zu finden.
Wählen Sie Textabschnitte aus um mit Künstlicher Intelligenz passenden Patente zu finden. powered by
Markieren Sie Textabschnitte, um KI-gestützt weitere passende Inhalte zu finden. powered by
Abstract
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.