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Insights into evolutionary interaction patterns of the 'Phosphorylation Activation Segment' in kinase


Adil Ahiri*,1, Hocine Garmes2, Crtomir Podlipnik3, Aziz Aboulmouhajir*,1,4



1Modeling and Molecular Spectroscopy Team, Faculty of Sciences, University Chouaib Doukkali, El-Jadida, Morroco; 2Analytical Chemistry and Environmental Sciences Team, Department of chemistry, Faculty of Science, University Chouaib Doukkali, El Jadida, Morroco; 3Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia; 4Extraction, Spectroscopy and Valorization Team, Organic synthesis, Extraction and Valorization Laboratory, Faculty of Sciences of Ain Chock, Hassan II University, Casablanca, Morocco.



Adil Ahiri - *Corresponding authors email: &


Article Type

Research Article



Received June 15, 2019; Revised October 7, 2019; Accepted October 9, 2019; Published October 13, 2019



We are interested in studying the phosphorylation of the kinase activation loop, distinguishing the passage from the unphosphorylated to the phosphorylated form without allostery. We performed an interaction study to trace the change of interactions between the activation segment and the kinase catalytic core, before and after phosphorylation. Results show that the structural changes are mainly due to the attraction between the phosphate group and guanidine groups of the arginine side chains of RD-pocket, which are constituted mainly of guanidine groups of the catalytic loop, the β9, and the αC helix. This attraction causes propagation of structural variation of the activation segment, principally towards the N-terminal. The structural variations are not made on all the amino acids of the activation segment; they are conditioned by the existence of two beta sheets stabilizing the loop during phosphorylation. The first, β6-β9 sheet is usually present in
most of the kinases; the second, β10-β11 is formed due to the interaction between the main chain amino acids of the activation loop and the αEF/αF loop.



Kinase, activation segment, phosphorylation, structural variation, interaction variation.



Ahiri et al. Bioinformation 15(9): 666-677 (2019)


Edited by

P Kangueane






Biomedical Informatics


License This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.