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ATP/ADP binding to a novel nucleotide binding domain of the reticulocyte-binding protein Py235 of Plasmodium yoelii

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ATP/ADP binding to a novel nucleotide binding domain of the reticulocyte-binding protein Py235 of Plasmodium yoelii

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dc.contributor.author Ramalingam, Jeya Kumar
dc.contributor.author Hunke, Cornelia
dc.contributor.author Gao, Xiaohong
dc.contributor.author Grüber, Gerhard
dc.contributor.author Preiser, Peter Rainer
dc.date.accessioned 2011-09-15T06:47:15Z
dc.date.available 2011-09-15T06:47:15Z
dc.date.copyright 2008
dc.date.issued 2011-09-15
dc.identifier.citation Ramalingam, J. K., Hunke, C., Gao, X., Grüber, G., & Preiser, P. R. (2008). ATP/ADP Binding to a Novel Nucleotide Binding Domain of the Reticulocyte-binding Protein Py235 of Plasmodium yoelii. Journal of Biological Chemistry, 283(52).
dc.identifier.issn 0021-9258
dc.identifier.uri http://hdl.handle.net/10220/7071
dc.description.abstract The mechanism by which a malaria merozoite recognizes a suitable host cell is mediated by a cascade of receptor-ligand interactions. In addition to the availability of the appropriate receptors, intracellular ATP plays an important role in determining whether erythrocytes are suitable for merozoite invasion. Recent work has shown that ATP secreted from erythrocytes signals a number of cellular processes. To determine whether ATP signaling might be involved in merozoite invasion, we investigated whether known plasmodium invasion proteins contain nucleotide binding motifs. Domain mapping identified a putative nucleotide binding region within all members of the reticulocyte-binding protein homologue (RBL) family analyzed. A representative domain, termed here nucleotide binding domain 94 (NBD94), was expressed and demonstrated to specifically bind to ATP. Nucleotide affinities of NBD94 were determined by fluorescence correlation spectroscopy, where an increase in the binding of ATP is observed compared with ADP analogues. ATP binding was reduced by the known F1F0-ATP synthase inhibitor 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Fluorescence quenching and circular dichroism spectroscopy of NBD94 after binding of different nucleotides provide evidence for structural changes in this protein. Our data suggest that different structural changes induced by ATP/ADP binding to RBL could play an important role during the invasion process.
dc.format.extent 11 p.
dc.language.iso en
dc.relation.ispartofseries Journal of biological chemistry
dc.rights © 2008 The American Society for Biochemistry and Molecular Biology. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Biological Chemistry, The American Society for Biochemistry and Molecular Biology. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [DOI: http://dx.doi.org/10.1074/jbc.M803102200].
dc.subject DRNTU::Science::Biological sciences::Microbiology::Virology.
dc.title ATP/ADP binding to a novel nucleotide binding domain of the reticulocyte-binding protein Py235 of Plasmodium yoelii
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1074/jbc.M803102200
dc.description.version Accepted version
dc.contributor.organization Agency for Science, Technology and Research (A*STAR)
dc.identifier.rims 161461

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