Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/60439
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Global conformational rearrangements during the activation of the GDP/GTP exchange factor Vav3 |
Autor: | Llorca, Óscar CSIC ORCID; Arias-Palomo, Ernesto CSIC ORCID ; Zugaza, José L.; Bustelo, Xosé R. CSIC ORCID | Fecha de publicación: | 2005 | Editor: | Nature Publishing Group | Citación: | EMBO Journal 24: 1330-1340 (2005) | Resumen: | Activation of Rho/Rac GTPases during cell signaling requires the participation of GDP/GTP exchange factors of the Dbl family. Although the structure of the catalytic core of Dbl proteins has been established recently, the molecular changes that the full-length proteins experience during normal or oncogenic conditions of stimulation are still unknown. Here, we have used single-particle electron microscopy to solve the structures of the inactive (unphosphorylated), active (phosphorylated), and constitutively active (N-terminally deleted) versions of the exchange factor Vav3. Comparison of these forms has revealed the interdomain interactions maintaining the inactive Vav3 state and the dynamic changes that the overall Vav3 structure undergoes upon tyrosine phosphorylation. We have also found that the conformations of phosphorylated Vav3 and N-terminally deleted Vav3 are distinct, indicating that the acquisition of constitutive activity by exchange factors is structurally more complex than the mere elimination of inhibitory interactions between structural domains. © 2005 European Molecular Biology Organization | All Rights Reserved. | URI: | http://hdl.handle.net/10261/60439 | DOI: | 10.1038/sj.emboj.7600617 | Identificadores: | doi: 10.1038/sj.emboj.7600617 issn: 0261-4189 e-issn: 1460-2075 |
Aparece en las colecciones: | (CIB) Artículos (IBMCC) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
21
checked on 24-abr-2024
SCOPUSTM
Citations
37
checked on 19-abr-2024
WEB OF SCIENCETM
Citations
32
checked on 23-feb-2024
Page view(s)
330
checked on 24-abr-2024
Download(s)
77
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.