alexa Three-dimensional Structure Prediction of the Human LMTK3 Catalytic Domain in DYG-in Conformation
ISSN: 2167-7956

Journal of Biomolecular Research & Therapeutics
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Research Article

Three-dimensional Structure Prediction of the Human LMTK3 Catalytic Domain in DYG-in Conformation

Loubna Allam1,2*, Wiame Lakhlili1, Zineb Tarhda1, Jihane Akachar1, Fatima Ghrifi1, Hamid El Amri2 and Azeddine Ibrahimi1

1Biotechnology Laboratory (MedBiotech), Rabat, Morocco

2Rabat Medical and Pharmacy School, Rabat, Morocco

*Corresponding Author:
Loubna Allam
Biotechnology Laboratory
Rabat, 10000, Morocco
Tel: +212 537 77 2850
Fax: 212 53 777 3701
E-mail: [email protected]

Received Date: April 10, 2017; Accepted Date: May 22, 2017; Published Date: May 29, 2017

Citation: Allam L, Lakhlili W, Tarhda Z, Akachar J, Ghrifi F, et al. (2017) Three-dimensional Structure Prediction of the Human LMTK3 Catalytic Domain in DYG-in Conformation. J Biomol Res Ther 6:151. doi: 10.4172/2167-7956.1000151

Copyright: © 2017 Allam L, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Lemur Tyrosine Kinase 3 (LMTK3) plays a key role in the regulation of α Estrogen Receptor (ERα) activity. It has been defined as an essential actor involved in the endocrine resistance process in breast cancer patients accelerating the dispersion and invasion of tumor cells which are the first steps of the metastatic process. In the absence of a crystallized structure of LMTK3 and in order to study its inhibition, we generated its tridimensional structure. We constructed the LMTK3 kinase in its active state (DYG-in) using the homology modeling approach. The evaluation of the generated model by several tools indicated the reliability of the predicted 3D structure and the good quality of the stereochemical characteristics model were confirmed by the PROCHECK tool. In conclusion, the docking approach used to study LMTK3-ATP interaction allows us to determine key residues of the ATP binding site that may be useful in the design of potential competitive ATP inhibitors of human LMTK3.

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