Computational Elucidation of Structural Basis for Ligand Binding with Leishmania donovani Adenosine Kinase.
Enzyme adenosine kinase is responsible for phosphorylation of adenosine to AMP and is crucial for parasites which are purine auxotrophs. The present study describes development of robust homology model of Leishmania donovani adenosine kinase to forecast interaction phenomenon with inhibitory molecul...
| Publicado en: | BioMed Research International Vol. 2013; pp. 609289 - 609290 |
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| Autores principales: | , , , , , , |
| Formato: | research Journal Article |
| Publicado: |
Wiley-Blackwell
2013
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=104090787&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 104090787 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 23146133 FT2T jtl: BioMed Research International issn: 23146133 maglogo: N pubinfo: dt: 2013 vid: 2013 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 104090787 104090787 2012240565 NLM23984386 PMC3741900 104090787 ppf: 609289 ppct: 1 formats: fmt: @attributes: type: P tig: atl: Computational Elucidation of Structural Basis for Ligand Binding with Leishmania donovani Adenosine Kinase. aug: au: Kar, Rajiv K Ansari, Md Yousuf Suryadevara, Priyanka Sahoo, Bikash R Sahoo, Ganesh C Dikhit, Manas R Das, Pradeep affil: Biomedical Informatics Centre, Rajendra Memorial Research Institute of Medical Science, Patna 800007, India ; Department of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), Hajipur 844102, India. sug: subj: Transferases Transferases Metabolism Leishmania Computer Simulation Amino Acids Chemistry, Physical Documentation Reproducibility of Results Proteins Human ab: Enzyme adenosine kinase is responsible for phosphorylation of adenosine to AMP and is crucial for parasites which are purine auxotrophs. The present study describes development of robust homology model of Leishmania donovani adenosine kinase to forecast interaction phenomenon with inhibitory molecules using structure-based drug designing strategy. Docking calculation using reported organic small molecules and natural products revealed key active site residues such as Arg131 and Asp16 for ligand binding, which is consistent with previous studies. Molecular dynamics simulation of ligand protein complex revealed the importance of hydrogen bonding with active site residues and solvent molecules, which may be crucial for successful development of drug candidates. Precise role of Phe168 residue in the active site was elucidated in this report that provided stability to ligandprotein complex via aromatic-re contacts. Overall, the present study is believed to provide valuable information to design a new compound with improved activity for antileishmanial therapeutics development. pubtype: Academic Journal doctype: research Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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