Structural similarities between the catalytic domain of threonine deaminase and the mammalian serine racemases

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Comparison of a newly found enzyme with its structural homologues results in the prediction of probable regulatory binding sites. Since serine racemases are found to be promising targets for the treatment of disorders related to NMDAR dysfunction [11], the identification of the structural similarities between serine racemases and their structural homologues might provide structural insights for rational drug design. In this study, we aim to determine the structural similarities between the mammalian serine racemases and the bacterial biosynthetic threonine deaminase.

Original languageEnglish (US)
Title of host publicationACE 2010 - 2010 International Conference on Advances in Computer Engineering
Pages371-373
Number of pages3
DOIs
StatePublished - 2010
Externally publishedYes
Event2010 International Conference on Advances in Computer Engineering, ACE 2010 - Bangalore, India
Duration: Jun 21 2010Jun 22 2010

Publication series

NameACE 2010 - 2010 International Conference on Advances in Computer Engineering

Conference

Conference2010 International Conference on Advances in Computer Engineering, ACE 2010
Country/TerritoryIndia
CityBangalore
Period6/21/106/22/10

Keywords

  • Domain
  • Homology
  • Serine racemases
  • Threonine deaminase

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