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dc.contributor.authorCapila, I.
dc.contributor.authorHernaiz, M.J.
dc.contributor.authorMo, Y.D.
dc.contributor.authorMealy, T.R.
dc.contributor.authorCampos, B.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorSeaton, B.A.
dc.date2001
dc.date.accessioned2022-06-27T16:20:26Z
dc.date.available2022-06-27T16:20:26Z
dc.date.issued2001-01-01
dc.identifier.citationAnnexin V-Heparin Oligosaccharide Complex Suggests Heparan Sulfate-Mediated Assembly on Cell Surfaces, I. Capila, M.J. Hernaiz, Y.D. Mo, T.R. Mealy, B. Campos, R.J. Linhardt B.A. Seaton, Structure, 9, 57-64, 2001.
dc.identifier.issn9692126
dc.identifier.urihttps://doi.org/10.1016/S0969-2126(00)00549-9
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5858
dc.descriptionStructure, 9, 57-64
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.abstractBackground: Annexin V, an abundant anticoagulant protein, has been proposed to exert its effects by self-assembling into highly ordered arrays on phospholipid membranes to form a protective anti-thrombotic shield at the cell surface. The protein exhibits very high-affinity calcium-dependent interactions with acidic phospholipid membranes, as well as specific binding to glycosaminoglycans (GAGs) such as heparin and heparan sulfate, a major component of cell surface proteoglycans. At present, there is no structural information to elucidate this interaction or the role it may play in annexin V function at the cell surface. Results: We report the 1.9 A crystal structure of annexin V in complex with heparin-derived tetrasaccharides. This structure represents the first of a heparin oligosaccharide binding to a protein where calcium ions are essential for the interaction. Two distinct GAG binding sites are situated on opposite protein surfaces. Basic residues at each site were identified from the structure and site-directed mutants were prepared. The heparin binding properties of these mutants were measured by surface plasmon resonance. The results confirm the roles of these mutated residues in heparin binding, and the kinetic and thermodynamic data define the functionally distinct character of each distal binding surface. Conclusion: The annexin V molecule, as it self-assembles into an organized array on the membrane surface, can bind the heparan sulfate components of cell surface proteoglycans. A novel model is presented in which proteoglycan heparan sulfate could assist in the localization of annexin V to the cell surface membrane and/or stabilization of the entire molecular assembly to promote anticoagulation.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/S0969-2126(00)00549-9
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.titleAnnexin V-Heparin Oligosaccharide Complex Suggests Heparan Sulfate-Mediated Assembly on Cell Surfaces
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/S0969-2126(00)00549-9
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/S0969-2126(00)00549-9
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.pages57-64
rpi.description.volume9


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