Exploration of the binding modes of L-asparaginase complexed with its amino acid substrates by molecular docking, dynamics and simulation.

ABSTRACT: Acute lymphocytic leukemia (ALL) is an outrageous disease worldwide. L-Asparagine (L-Asn) and L-glutamine (L-Gln) deamination plays crucial role in ALL treatment. Role of Erwinaze^® (L-asparaginase from Erwinia chrysanthemi) in regulation of L-Asn and L-Gln has been confirmed by the experimental studies. Therapeutic research against ALL remained elusive with the lack of structural information on Erwinaze^® enzyme. In this present study, homology model of the Erwinaze^® was developed using MODELLER and the same was validated by various quality indexing tools. For the apo state enzyme and ligand bound state complexes molecular dynamics (MD) simulation was performed. The trajectory analysis showed the confirmational changes of structures in the dynamic system. Li

SUBMITTER: Reddy ER 

PROVIDER: S-EPMC4835421 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature