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Título

3D structure of Syk kinase determined by single-particle electron microscopy

Autor Arias-Palomo, Ernesto ; Recuero-Checa, María Ángeles ; Bustelo, Xosé R.; Llorca, Óscar
Palabras clave Single-particle electron microscopy
EM
Syk
Zap-70
Kinases
Fecha de publicación 26-oct-2007
EditorElsevier
Citación Biochimica et Biophysica Acta 1774(12):1493-1499(2007)
ResumenThe cytoplasmic Syk kinase plays key roles in immune responses and comprises two N-terminal regulatory Src homology 2 (SH2) domains followed by a catalytic region. Atomic structures of these domains have only been solved in isolation. To gain insights into the three-dimensional structure of full-length Syk, we have used single-particle electron microscopy. Syk acquires a closed conformation resembling the inhibited structure of Zap-70, another member of the Syk family. Such configuration suggests an inhibition of the N-terminal domains on its catalytic activity. The phosphotyrosine binding pockets of both SH2 domains are not occluded and they could interact with other phosphoproteins.
Descripción 7 pages, 3 figures.-- PMID: 18021750 [PubMed].-- PMCID: PMC2186377.-- Printed version published Dec 2007.-- Supplementary information (suppl. figure S1) available at the publisher website.
Versión del editorhttp://dx.doi.org/10.1016/j.bbapap.2007.10.008
URI http://hdl.handle.net/10261/9589
DOI10.1016/j.bbapap.2007.10.008
ISSN0167-4889
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