2021
A structurally preserved allosteric site in the MIF superfamily affects enzymatic activity and CD74 activation in D-dopachrome tautomerase
Chen E, Reiss K, Shah D, Manjula R, Allen B, Murphy EL, Murphy JW, Batista VS, Bhandari V, Lolis EJ, Lisi GP. A structurally preserved allosteric site in the MIF superfamily affects enzymatic activity and CD74 activation in D-dopachrome tautomerase. Journal Of Biological Chemistry 2021, 297: 101061. PMID: 34384784, PMCID: PMC8405996, DOI: 10.1016/j.jbc.2021.101061.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric SiteAmino Acid SequenceAntigens, Differentiation, B-LymphocyteBinding SitesCatalytic DomainCrystallography, X-RayCytokinesHistocompatibility Antigens Class IIHumansIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsProtein BindingStructure-Activity RelationshipConceptsAllosteric siteDopachrome tautomeraseDynamic regulatory networksEnzymatic activityLow sequence identityLigand-binding siteMultiple ligand-binding sitesNonoverlapping functionsRegulatory networksAllosteric couplingMacrophage migration inhibitory factor (MIF) familyFactor familySequence identityHomolog DStructural basisPrimary sequenceCD74 activationFunctional similarityConformational changesSolution NMRMIF-2X-ray crystallographyCatalytic siteStructural consequencesSolvent channels
2016
Identification of New Inhibitors for Human SIRT1: An in-silico Approach.
Padmanabhan B, Ramu M, Mathur S, Unni S, Thiyagarajan S. Identification of New Inhibitors for Human SIRT1: An in-silico Approach. Medicinal Chemistry 2016, 12: 347-61. PMID: 26740209, DOI: 10.2174/1573406412666160107111612.Peer-Reviewed Original ResearchConceptsMolecular dynamics simulationsDynamics simulationsNew chemical librariesInhibitor compoundsChemical librariesCrystal structureStructure-based methodsUseful scaffoldsVirtual screeningChemical classesAutoDock VinaCompoundsNew inhibitorsDiphenylNew classSilico approachInhibitory activityTreatment of cancerComplex structureStructureDerivativesVinaScaffoldsAvailable drugsHuman SIRT1