NMR structural determinants of eosinophil cationic protein binding to membrane and heparin mimetics

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  • dc.contributor.author García Mayoral, María Florca
  • dc.contributor.author Moussaoui, Mohammedca
  • dc.contributor.author Torre, Beatriz G. de laca
  • dc.contributor.author Andreu Martínez, Davidca
  • dc.contributor.author Boix, Esterca
  • dc.contributor.author Nogués, Victòria M.ca
  • dc.contributor.author Rico, Manuelca
  • dc.contributor.author Laurents, Douglas V.ca
  • dc.contributor.author Bruix, Martaca
  • dc.date.accessioned 2016-01-07T15:07:57Z
  • dc.date.available 2016-01-07T15:07:57Z
  • dc.date.issued 2010
  • dc.description.abstract Eosinophil cationic protein (ECP) is a highly stable, cytotoxic ribonuclease with the ability to enter and disrupt membranes that participates in innate immune defense against parasites but also kills human cells. We have used NMR spectroscopy to characterize the binding of ECP to membrane and heparin mimetics at a residue level. We believe we have identified three Arg-rich surface loops and Trp(35) as crucial for membrane binding. Importantly, we have provided evidence that the interaction surface of ECP with heparin mimetics is extended with respect to that previously described (fragment 34-38). We believe we have identified new sites involved in the interaction for the first time, and shown that the N-terminal alpha-helix, the third loop, and the first and last beta-strands are key for heparin binding. We have also shown that a biologically active ECP N-terminal fragment comprising the first 45 residues (ECP1-45) retains the capacity to bind membrane and heparin mimetics, thus neither the ECP tertiary structure nor its high conformational stability are required for cytotoxicity.ca
  • dc.description.sponsorship This work was supported by the Spanish Ministerio de Ciencia e Innovación (CTQ2008-00080/BQU, BIO2008-04487-CO3-02, BFU2006-15543-CO2-01, BFU2009-09371).
  • dc.format.mimetype application/pdfca
  • dc.identifier.citation García-Mayoral MF, Moussaoui M, de la Torre BG, Andreu D, Boix E, Nogués MV et al. NMR structural determinants of eosinophil cationic protein binding to membrane and heparin mimetics. Biophysical journal. 2010;98(11):2702-11. DOI: 10.1016/j.bpj.2010.02.039ca
  • dc.identifier.doi http://dx.doi.org/10.1016/j.bpj.2010.02.039
  • dc.identifier.issn 0006-3495
  • dc.identifier.uri http://hdl.handle.net/10230/25538
  • dc.language.iso engca
  • dc.publisher Elsevierca
  • dc.relation.ispartof Biophysical journal. 2010;98(11):2702-11
  • dc.rights © Elsevier. This is the published version of an article http://dx.doi.org/10.1016/j.bpj.2010.02.039 that appeared in the journal Biophysical journal. It is published in an Open Archive under an Elsevier user license. Details of this licence are available here: http://www.elsevier.com/about/open-access/open-access-policies/oa-license-policy/elsevier-user-licenseca
  • dc.rights.accessRights info:eu-repo/semantics/openAccessca
  • dc.subject.other Proteïnes -- Estructuraca
  • dc.subject.other Pèptidsca
  • dc.title NMR structural determinants of eosinophil cationic protein binding to membrane and heparin mimeticsca
  • dc.type info:eu-repo/semantics/articleca
  • dc.type.version info:eu-repo/semantics/publishedVersionca

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