structural elucidation of the dfg-asp in and dfg-asp out states of tam kinases and insight into the selectivity of their inhibitors

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ID: 213590
2014
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Abstract
Structural elucidation of the active (DFG-Asp in) and inactive (DFG-Asp out) states of the TAM family of receptor tyrosine kinases is required for future development of TAM inhibitors as drugs. Herein we report a computational study on each of the three TAM members Tyro-3, Axl and Mer. DFG-Asp in and DFG-Asp out homology models of each one were built based on the X-ray structure of c-Met kinase, an enzyme with a closely related sequence. Structural validation and in silico screening enabled identification of critical amino acids for ligand binding within the active site of each DFG-Asp in and DFG-Asp out model. The position and nature of amino acids that differ among Tyro-3, Axl and Mer, and the potential role of these residues in the design of selective TAM ligands, are discussed.
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messoussi2014moleculesstructural Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Abdellah Messoussi;Lucile Peyronnet;Clémence Feneyrolles;Gwénaël Chevé;Khalid Bougrin;Aziz Yasri
Journal Journal of ethnopharmacology
Year 2014
DOI
10.3390/molecules191016223
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