http://opendata.unex.es/recurso/ciencia-tecnologia/investigacion/publicaciones/Publicacion/2003-324
Literals
- dcterms:title
- Involvement of the cytoplasmic loop L6-7 in the entry mechanism for transport of Ca<sup>2+</sup> through the sarcoplasmic reticulum Ca<sup>2+</sup>-ATPase
- ou:eid
- bibo:doi
- 10.1111/j.1749-6632.2003.tb07143.x
- 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}}
- dcterms:creator
- dcterms:contributor
- Corre, F., Jaxel, C., Fuentes, J., Menguy, T., Falson, P., Levine, B.A., Møller, J.V., Le Maire, M.
- fabio:hasPublicationYear
- vivo:identifier
- bibo:issn
- bibo:page_range
- dcterms:publisher
- Annals of the New York Academy of Sciences
- ou:tipoPublicacion
- vcard:url
- ou:urlScopus
- ou:vecesCitado
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