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dc.contributor.authorMcArdle, Bernadette M
dc.contributor.authorQuinn, Ronald J
dc.date.accessioned2017-05-03T14:07:12Z
dc.date.available2017-05-03T14:07:12Z
dc.date.issued2007
dc.date.modified2009-12-02T05:53:01Z
dc.identifier.issn1439-4227
dc.identifier.doi10.1002/cbic.200700035
dc.identifier.urihttp://hdl.handle.net/10072/17795
dc.description.abstractNatural products have withstood the test of time as therapeutics, but new lead-generation strategies have focussed away from natural products. A new approach that uses natural-product recognition to drive an understanding of biological space might provide an impetus for renewed focus on natural-product starting points. Protein fold topology (PFT) has been shown to be an underlying factor for natural-product recognition. An investigation of natural product inhibitors of the Zincin-like fold has demonstrated their capacity also to inhibit targets of different fold types. Analysis of crystal structure complexes for natural products cocrystallised within different fold types has shown similarity at the PFT level. Two new PFTT (where subscript T denotes PFT shared between therapeutic targets) relationships have been established: the Zincin-like- metallohydrolase/oxidoreductase PFTT and the Zincin-like-phosphorylase/hydrolase PFTT. The PFT relationship between a natural product's biosynthetic enzyme and therapeutic target, and now between different fold targets of the same natural product, suggests that PFT is the simplest descriptor of biological space. This fundamental factor for recognition could facilitate a rational approach to drug development guided by natural products.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley-VCH Verlag GmbH & Co. KGaA
dc.publisher.placeGermany
dc.publisher.urihttps://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.200700035
dc.relation.ispartofstudentpublicationY
dc.relation.ispartofpagefrom788
dc.relation.ispartofpageto798
dc.relation.ispartofissue7
dc.relation.ispartofjournalChemBioChem
dc.relation.ispartofvolume8
dc.rights.retentionY
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3101
dc.titleIdentification of Protein Fold Topology Shared between Different Folds Inhibited by Natural Products
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.rights.copyrightSelf-archiving of the author-manuscript version is not yet supported by this publisher. Please refer to the journal link for access to the definitive, published version or contact the author for more information.
gro.date.issued2007
gro.hasfulltextNo Full Text
gro.griffith.authorQuinn, Ronald J.


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