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dc.contributor.authorFox, Jamie C.
dc.contributor.authorTyler, Robert C.
dc.contributor.authorPeterson, Francis C.
dc.contributor.authorDyer, Douglas P.
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorHandel, Tracy M.
dc.contributor.authorVolkman, Brian F.
dc.date2016
dc.date.accessioned2022-06-23T04:20:07Z
dc.date.available2022-06-23T04:20:07Z
dc.date.issued2016-03-01
dc.identifier.citationExamination of glycosaminoglycan binding sites on the XCL1 dimer, J. C. Fox, R. C. Tyler, F. C. Peterson, D. P. Dyer, F. Zhang, R. J. Linhardt, T. M. Handel, B. F. Volkman, Biochemistry, 55, 1214–1225, 2016.
dc.identifier.issn15204995
dc.identifier.issn62960
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5348
dc.identifier.urihttps://doi.org/10.1021/acs.biochem.5b01329
dc.descriptionBiochemistry, 55, 1214–1225
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractKnown for its distinct metamorphic behavior, XCL1 interconverts between a canonical chemokine folded monomer (XCL1mon) that interacts with the receptor, XCR1, and a unique dimer (XCL1dim) that interacts with glycosaminoglycans and inhibits HIV-1 activity. This study presents the first detailed analysis of the GAG binding properties of XCL1dim. Basic residues within a conformationally selective dimeric variant of XCL1 (W55D) were mutated and analyzed for their effects on heparin binding. Mutation of Arg23 and Arg43 greatly diminished the level of heparin binding in both heparin Sepharose chromatography and surface plasmon resonance assays. To assess the contributions of different GAG structures to XCL1 binding, we developed a solution fluorescence polarization assay and correlated affinity with the length and level of sulfation of heparan sulfate oligosaccharides. It was recently demonstrated that the XCL1 GAG binding form, XCL1dim, is responsible for preventing HIV-1 infection through interactions with gp120. This study defines a GAG binding surface on XCL1dim that includes residues that are important for HIV-1 inhibition.
dc.description.sponsorshipNational Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherAmerican Chemical Society (ACS)
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleExamination of glycosaminoglycan binding sites on the XCL1 dimer
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/acs.biochem.5b01329
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages1214-1225
rpi.description.volume55


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