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dc.contributor.authorFulcher, Yan G.
dc.contributor.authorPrior, Stephen H.
dc.contributor.authorMasuko, Sayaka
dc.contributor.authorLi, Lingyun
dc.contributor.authorPu, Dennis
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorVan Doren, Steven R.
dc.date2017
dc.date.accessioned2022-06-27T16:01:10Z
dc.date.available2022-06-27T16:01:10Z
dc.date.issued2017-07-05
dc.identifier.citationGlycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7, Y. G. Fulcher, S. H. Prior, S. Masuko, L. Li, D. Pu, F. Zhang, R. J. Linhardt, S. R. Van Doren, Structure, 25, 1100–1110, 2017.
dc.identifier.issn18784186
dc.identifier.issn9692126
dc.identifier.urihttps://doi.org/10.1016/j.str.2017.05.019
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5622
dc.descriptionStructure, 25, 1100–1110
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.abstractHeparan sulfate proteoglycans activate the matrix metalloproteinase-7 zymogen (proMMP-7) and recruit it in order to shed proteins from cell surfaces. This occurs in uterine and mammary epithelia, bacterial killing, lung healing, and tumor cell signaling. Basic tracks on proMMP-7 recognize polyanionic heparin, according to nuclear magnetic resonance and mutations disruptive of maturation. Contacts and proximity measurements guided docking of a heparin octasaccharide to proMMP-7. The reducing end fits into a basic pocket in the pro-domain while the chain continues toward the catalytic domain. Another oligosaccharide traverses a basic swath remote on the catalytic domain and inserts its reducing end into a slot formed with the basic C terminus. This latter association appears to support allosteric acceleration of proteolysis. The modes of binding account for extended, heterogeneous assemblies of proMMP-7 with heparinoids during maturation and for bridging to pro-α-defensins and proteoglycans. These associations support proteolytic release of activities at epithelial cell surfaces.
dc.description.sponsorshipNational Institutes of Health
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.str.2017.05.019
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofStructure
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleGlycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.str.2017.05.019
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dcterms.isVersionOfhttps://doi.org/10.1016/j.str.2017.05.019
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.pages1100-1110.e5
rpi.description.volume25


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