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Determination and validation of mTOR kinase-domain 3D structure by homology modeling

Wiame Lakhlili1, Gwénaël Chevé2, Abdelaziz Yasri2

  • 1Laboratoire de Biotechnologie (MedBiotech), Faculté de Médecine et de Pharmacie de Rabat, Université Mohammed V de Rabat, Rabat, Morroco.

Oncotargets and Therapy
|August 11, 2015
PubMed

Insights

This study presents a validated 3D model of the mammalian target of rapamycin (mTOR) catalytic site. This structural insight aids in understanding cancer-related signaling pathways and developing targeted therapies.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cancer Signaling

Background:

  • The AKT/mammalian target of rapamycin (mTOR) pathway is frequently activated in human cancers.
  • mTOR functions within two distinct complexes: mTORC1 (with Raptor) and mTORC2 (with Rictor).

Purpose of the Study:

  • To develop and validate a three-dimensional (3D) structural model of the mTOR catalytic region.
  • To provide a structural basis for understanding mTOR deregulation in cancer.

Main Methods:

  • Homology modeling using the SWISS-MODEL program based on the PI3Kγ crystal structure.
  • Model quality assessment and validation with PROCHECK, PROVE, and Ramachandran plot analysis.
  • Inhibitor docking studies to further validate the model's accuracy.

Main Results:

  • A validated 3D model of the mTOR catalytic site was successfully generated.
  • Stereochemical properties and overall structure quality were confirmed through rigorous validation methods.
  • Docking simulations supported the reliability of the developed mTOR model.

Conclusions:

  • The presented 3D model offers a reliable structural representation of the mTOR catalytic site.
  • This validated model can serve as a valuable tool for future drug discovery and cancer research targeting the mTOR pathway.
Keywords:
dockinghomology modelingmTORmTOR kinase-domain

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