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Insight into TPMT(∗)23 mutation mis-folding using molecular dynamics simulation and protein structure analysis.

Sofiene Larif1, Chaker Ben Salem, Zohra Soua

  • 1a Faculty of Medicine of Sousse, Metabolic Biophysics and Applied Pharmacology Laboratory, Department of Biophysics , Avenue Mohamed Karoui , Sousse , 4002 , Tunisia.

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Thiopurine S-methyltransferase (TPMT) enzyme activity is affected by the rare TPMT*23 polymorphism. This study reveals how the A167G substitution alters protein structure, impacting drug metabolism.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacogenomics

Background:

  • Thiopurine S-methyltransferase (TPMT) is crucial for metabolizing thiopurine drugs.
  • TPMT exhibits significant interindividual polymorphism, affecting drug efficacy and safety.
  • The rare TPMT*23 polymorphism's structural basis and functional impact remain unclear.

Purpose of the Study:

  • To elucidate the structural basis of the TPMT*23 polymorphism.
  • To investigate the molecular mechanisms by which the A167G substitution affects TPMT enzyme activity.
  • To provide a genetic prediction of the mutation's functional consequences.

Main Methods:

  • Analysis of wild-type (WT) TPMT protein structure.
  • Identification of amino acids bordering water channels in thiopurine sites.
  • Molecular dynamics simulations of WT and TPMT*23 variants.
  • Investigation of structural modifications and hydrogen bond alterations.
  • Genetic prediction of mutation functional consequences.

Main Results:

  • The A167G substitution in TPMT*23 propagates through hydrogen bond alterations.
  • Structural modifications affect both thiopurine and S-adenosylmethionine binding sites.
  • The thiopurine site's pincer-like closure mechanism is impacted.
  • Functional consequences of the mutation were predicted, confirming altered enzyme activity.

Conclusions:

  • The TPMT*23 polymorphism, caused by A167G substitution, leads to significant structural changes affecting enzyme function.
  • Understanding these structural alterations is key to predicting TPMT drug metabolism variations.
  • This research clarifies the molecular basis of a rare TPMT variant, aiding personalized medicine approaches.