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<https://opendata.unex.es/recurso/ciencia-tecnologia/investigacion/publicaciones/Publicacion/2003-324> vivo:identifier "2003-324";
    bibo:doi "10.1111/j.1749-6632.2003.tb07143.x";
    ou:tipoPublicacion "Conference Paper";
    dcterms:publisher "Annals of the New York Academy of Sciences";
    vcard:url <https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0038579556&origin=inward>;
    ou:eid "2-s2.0-0038579556";
    dcterms:title "Involvement of the cytoplasmic loop L6-7 in the entry mechanism for transport of Ca2+ through the sarcoplasmic reticulum Ca2+-ATPase";
    fabio:hasPublicationYear "2003";
    dcterms:creator "Corre F.";
    dcterms:contributor "Corre, F.; Jaxel, C.; Fuentes, J.; Menguy, T.; Falson, P.; Levine, B.A.; Møller, J.V.; Le Maire, M.";
    ou:bibtex "@inproceedings{ISI:000183407000014, Author= {Corre, F and Jaxel, C and Fuentes, J and Menguy, T and Falson, P and Levine, BA and Moller, JV and Le Maire, M}, Editor= {Jorgensen, PL and Karlish, SJD and Maunsbach, AB}, Title= {Involvement of the cytoplasmic loop L6-7 in the entry mechanism for transport of Ca2+ through the sarcoplasmic reticulum Ca2+-ATPase}, Booktitle= {NA,K-ATPASE AND RELATED CATION PUMPS: STRUCTURE, FUNCTION, AND REGULATORY MECHANISMS}, Series= {ANNALS OF THE NEW YORK ACADEMY OF SCIENCES}, Year= {2003}, Volume= {986}, Pages= {90-95}, Note= {10th International Conference on Na,K-ATPase and Related Cation Pumps, ELSINORE, DENMARK, AUG 08-14, 2002}, Abstract= {We have found that despite a markedly low calcium affinity the D813A/D818A mutant is capable, after complexation with Cr.ATP, of occluding Ca2+ to the same extent (1-2 Ca2+ per ATPase monomer) as wild- type ATPase. The inherent ability of the synthetic L6-7 loop peptide to bind Ca2+ was demonstrated with murexide and mass spectrometry. NMR analysis indicated the formation of specific 1:1 cation complexes of the peptide with calcium and lanthanum with coordination by all three aspartate residues D813/D815/D818 that resulted in an altered conformation of the peptide chain. Overall our observations suggest that, in addition to mediating contact between the intramembranous Ca2+ binding sites and the cytosotic phospho lation site as previously suggested, the L6-7 loop, in a preceding step, participates in the formation of an entrance port important for lodging Ca2+ at a high-affinity binding site inside the membrane.}, Publisher= {NEW YORK ACAD SCIENCES}, Address= {2 EAST 63RD ST, NEW YORK, NY 10021 USA}, Type= {Article; Proceedings Paper}, Language= {English}, Affiliation= {Le Maire, M (Reprint Author), CEA Saclay, Biophys Sect, Dept Biol Joliot Curie, Bat 528, F-91191 Gif Sur Yvette, France. CEA Saclay, Biophys Sect, Dept Biol Joliot Curie, F-91191 Gif Sur Yvette, France. CEA Saclay, CNRS, URA 2096, F-91191 Gif Sur Yvette, France. Univ Paris 06, LRA17V, F-91191 Gif Sur Yvette, France. Univ Extremadura, Dept Bioquim \\& Biol Mol \\& Genet, EU Enfermeria \\& TO, Caceres, Spain. Univ Birmingham, Sch Biosci, Birmingham B15 2TT, W Midlands, England. Aarhus Univ, Dept Biophys, DK-8000 Aarhus C, Denmark.}, ISSN= {0077-8923}, ISBN= {1-57331-401-3}, Keywords= {Ca2+ ATPase; loop NMR structure}, Keywords-Plus= {TRANSMEMBRANE SEGMENT-6; CALCIUM-PUMP}, Research-Areas= {Biochemistry \\& Molecular Biology; Science \\& Technology - Other Topics}, Web-of-Science-Categories= {Biochemistry \\& Molecular Biology; Multidisciplinary Sciences}, ResearcherID-Numbers= {Fuentes, Jose/H-9490-2014}, ORCID-Numbers= {Fuentes, Jose/0000-0001-6910-2089}, Number-of-Cited-References= {7}, Times-Cited= {1}, Journal-ISO= {Ann.NY Acad.Sci.}, Doc-Delivery-Number= {BW85L}, Unique-ID= {ISI:000183407000014}}";
    bibo:volume "986";
    dcterms:created "2003-01-01T00:00:00"^^xsd:dateTime;
    ou:urlScopus <https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0038579556&origin=inward>;
    a ou:Publicacion;
    ou:vecesCitado "1";
    bibo:issn "0077-8923";
    bibo:page_range "90-95".
<https://opendata.unex.es/recurso/educacion/universidad/personal/e529f24d85062c120b2d2ce7f35780c0-jose-manuel-fuentes-rodriguez> ou:tienePublicacion <https://opendata.unex.es/recurso/ciencia-tecnologia/investigacion/publicaciones/Publicacion/2003-324>.