Structural studies of human purine nucleoside phosphorylase: Towards a new specific empirical scoring function

dc.creatorTimmers, LFSM
dc.creatorCaceres, RA
dc.creatorVivan, AL
dc.creatorGava, LM
dc.creatorDias, R
dc.creatorDucati, RG
dc.creatorBasso, LA
dc.creatorSantos, DS
dc.creatorde Azevedo, WF
dc.date2008
dc.date37196
dc.date2014-07-31T14:26:18Z
dc.date2015-11-26T17:04:58Z
dc.date2014-07-31T14:26:18Z
dc.date2015-11-26T17:04:58Z
dc.date.accessioned2018-03-28T23:53:18Z
dc.date.available2018-03-28T23:53:18Z
dc.identifierArchives Of Biochemistry And Biophysics. Elsevier Science Inc, v. 479, n. 1, n. 28, n. 38, 2008.
dc.identifier0003-9861
dc.identifierWOS:000260593400004
dc.identifier10.1016/j.abb.2008.08.015
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/75471
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/75471
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1279462
dc.descriptionHuman purine nucleoside phosphorylase (HsPNP) is a target for inhibitor development aiming at T-cell immune response modulation. In this work, we report the development of a new set of empirical scoring functions and its application to evaluate binding affinities and docking results. To test these new functions, we solved the structure of HsPNP and 2-mercapto-4(3H)-quinazolinone (HsPNP:MQU) binary complex at 2.7 A resolution using synchrotron radiation, and used these functions to predict ligand position obtained in Clocking Simulations. We also employed molecular dynamics simulations to analyze HsPNP in two conditions, as apoenzyme and in the binary complex form, in order to assess the structural features responsible for stability. Analysis of the Structural differences between systems provides explanation for inhibitor binding. The use of these scoring functions to evaluate binding affinities and molecular docking results may be used to guide future efforts on virtual screening focused on HsPNP. (c) 2008 Elsevier Inc. All rights reserved.
dc.description479
dc.description1
dc.description28
dc.description38
dc.languageen
dc.publisherElsevier Science Inc
dc.publisherNew York
dc.publisherEUA
dc.relationArchives Of Biochemistry And Biophysics
dc.relationArch. Biochem. Biophys.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectEmpirical scoring functions
dc.subjectDocking
dc.subjectVirtual screening
dc.subjectQuinazolinone
dc.subjectEnzymology
dc.subjectMolecular dynamics
dc.subjectMolecular-dynamics Simulations
dc.subjectParticle-mesh Ewald
dc.subjectCrystal-structure
dc.subjectAngstrom Resolution
dc.subjectCalf Thymus
dc.subjectFree-energy
dc.subjectInhibitor
dc.subjectProteins
dc.subjectBinding
dc.subjectPnp
dc.titleStructural studies of human purine nucleoside phosphorylase: Towards a new specific empirical scoring function
dc.typeArtículos de revistas


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