HIGH QUALITY SCIENTIFIC CONTENT,  ONLINE OPEN ACCESS,  GLOBAL SCIENTIFIC AUDIENCE,  COST EFFECTIVE, ANY ONE CAN DOWNLOAD REPRINTS 
Spreading knowledge

Google Scholar

Google Scholar

Archives

Back 

USE OF CRYSTALLOGRAPHIC STRUCTURE IN MOLECULAR MODELLING FOR DIPEPTIDYL PEPTIDASE SERIES. Pinku Mehto, Vivek Kumar, Vivek Gupta, Pardeep Kumar, Saroj Basnet, Gurvinder Singh

USE OF CRYSTALLOGRAPHIC STRUCTURE IN MOLECULAR MODELLING FOR DIPEPTIDYL PEPTIDASE SERIES.

Pinku Mehto, Vivek Kumar, Vivek Gupta, Pardeep Kumar, Saroj Basnet, Gurvinder Singh


International Journal of Natural Product Science 2012: Spl Issue 1:109.

Abstract(RBIP-109)

We report the development of homology models of dipeptidyl peptidase series (DPP-8 and DPP-9) based on the high resolution crystal structure of available DPP-IV enzyme. The model was built by taking template of human DPP-IV enzyme and quality of model structures are verified by Procheck. The homology models were built and refined using MOE modeling mode where the active sites were optimized by the help of OPLS-AA forcefield to allow side chain flexibility alongwith further optimization and refinement. The location of active site residues and active site structural elements between template and target revealed difference in selectivity pattern of dipeptidyl peptidase enzymes. Finally, the molecular docking studies provide detail observation in binding of ligands in DPP series. The result may help to analyze actual selectivity pattern of dipeptidyl peptidase enzymes and an opportunity for the development of anti-diabetic agents targeting only human DPP-IV enzyme.

Keywords: Modelling, DPP-IV, forcefield, MOE, GB/SA, Protonation, PRALINE, Docking, Template, Active site
Attachments:
Time to create page: 0.12 seconds


Copyright © All rights reserved Science Instinct Publications sciipub.com