Small-Angle X-ray Scattering Models of APOBEC3B Catalytic Domain in a Complex with a Single-Stranded DNA Inhibitor

Simple item page
dc.citation.issue2
dc.citation.volume13
dc.contributor.authorBarzak FM
dc.contributor.authorRyan TM
dc.contributor.authorKvach MV
dc.contributor.authorKurup HM
dc.contributor.authorAihara H
dc.contributor.authorHarris RS
dc.contributor.authorFilichev VV
dc.contributor.authorHarjes E
dc.contributor.authorJameson GB
dc.contributor.editorChelico L
dc.coverage.spatialSwitzerland
dc.date.accessioned2023-11-12T19:50:28Z
dc.date.accessioned2023-11-20T01:38:09Z
dc.date.available2021-02-12
dc.date.available2023-11-12T19:50:28Z
dc.date.available2023-11-20T01:38:09Z
dc.date.issued2021-02-12
dc.description.abstractIn normal cells APOBEC3 (A3A-A3H) enzymes as part of the innate immune system deaminate cytosine to uracil on single-stranded DNA (ssDNA) to scramble DNA in order to give protection against a range of exogenous retroviruses, DNA-based parasites, and endogenous retroelements. However, some viruses and cancer cells use these enzymes, especially A3A and A3B, to escape the adaptive immune response and thereby lead to the evolution of drug resistance. We have synthesized first-in-class inhibitors featuring modified ssDNA. We present models based on small-angle X-ray scattering (SAXS) data that (1) confirm that the mode of binding of inhibitor to an active A3B C-terminal domain construct in the solution state is the same as the mode of binding substrate to inactive mutants of A3A and A3B revealed in X-ray crystal structures and (2) give insight into the disulfide-linked inactive dimer formed under the oxidizing conditions of purification.
dc.description.confidentialfalse
dc.edition.editionFebruary 2021
dc.format.pagination290-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/33673243
dc.identifier.citationBarzak FM, Ryan TM, Kvach MV, Kurup HM, Aihara H, Harris RS, Filichev VV, Harjes E, Jameson GB. (2021). Small-Angle X-ray Scattering Models of APOBEC3B Catalytic Domain in a Complex with a Single-Stranded DNA Inhibitor.. Viruses. 13. 2. (pp. 290-).
dc.identifier.doi10.3390/v13020290
dc.identifier.eissn1999-4915
dc.identifier.elements-typejournal-article
dc.identifier.issn1999-4915
dc.identifier.numberARTN 290
dc.identifier.piiv13020290
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/69160
dc.languageeng
dc.publisherMDPI (Basel, Switzerland)
dc.publisher.urihttps://www.mdpi.com/1999-4915/13/2/290
dc.relation.isPartOfViruses
dc.rightsCC BY
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectAPOBEC
dc.subjectAPOBEC inhibitors
dc.subjectAPOBEC3
dc.subjectAPOBEC3B
dc.subjectSAXS
dc.subjectcancer evolution
dc.subjectdimer
dc.subjectdrug resistance
dc.subjectvirus restriction
dc.subjectCatalytic Domain
dc.subjectCytidine Deaminase
dc.subjectDNA, Single-Stranded
dc.subjectDimerization
dc.subjectHumans
dc.subjectMinor Histocompatibility Antigens
dc.subjectMutation
dc.subjectRNA, Viral
dc.subjectRetroviridae
dc.subjectRetroviridae Infections
dc.subjectScattering, Small Angle
dc.titleSmall-Angle X-ray Scattering Models of APOBEC3B Catalytic Domain in a Complex with a Single-Stranded DNA Inhibitor
dc.typeJournal article
pubs.elements-id440933
pubs.organisational-groupOther
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
440933 PDF.pdf
Size:
31.06 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Journal Articles