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dc.contributor.authorSturm, Noe
dc.contributor.authorQuinn, Ronald J
dc.contributor.authorKellenberger, Esther
dc.date.accessioned2017-11-28T04:14:30Z
dc.date.available2017-11-28T04:14:30Z
dc.date.issued2015
dc.identifier.issn0032-0943
dc.identifier.doi10.1055/s-0035-1545697
dc.identifier.urihttp://hdl.handle.net/10072/101204
dc.description.abstractNatural products are made by nature through interaction with biosynthetic enzymes. They also exert their effect as drugs by interaction with proteins. To address the question “Do biosynthetic enzymes and therapeutic targets share common mechanisms for the molecular recognition of natural products?”, we compared the active site of five flavonoid biosynthetic enzymes to 8077 ligandable binding sites in the Protein Data Bank using two three-dimensional-based methods (SiteAlign and Shaper). Virtual screenings efficiently retrieved known flavonoid targets, in particular protein kinases. A consistent performance obtained for variable site descriptions (presence/absence of water, variable boundaries, or small structural changes) indicated that the methods are robust and thus well suited for the identification of potential target proteins of natural products. Finally, our results suggested that flavonoid binding is not primarily driven by shape, but rather by the recognition of common anchoring points.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherGeorg Thieme Verlag KG
dc.relation.ispartofpagefrom467
dc.relation.ispartofpageto473
dc.relation.ispartofissue6
dc.relation.ispartofjournalPlanta Medica
dc.relation.ispartofvolume81
dc.subject.fieldofresearchPlant Biology not elsewhere classified
dc.subject.fieldofresearchPlant Biology
dc.subject.fieldofresearchComplementary and Alternative Medicine
dc.subject.fieldofresearchPharmacology and Pharmaceutical Sciences
dc.subject.fieldofresearchcode060799
dc.subject.fieldofresearchcode0607
dc.subject.fieldofresearchcode1104
dc.subject.fieldofresearchcode1115
dc.titleSimilarity between flavonoid biosynthetic enzymes and flavonoid protein targets captured by three-dimensional computing approach
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyGriffith Sciences, Griffith Institute for Drug Discovery
gro.hasfulltextNo Full Text
gro.griffith.authorQuinn, Ronald J.
gro.griffith.authorSturm, Noe


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