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

AuthorsArias-Palomo, Ernesto ; Recuero-Checa, María Ángeles ; Bustelo, Xosé R. ; Llorca, Óscar
KeywordsSingle-particle electron microscopy
Issue Date26-Oct-2007
CitationBiochimica et Biophysica Acta 1774(12):1493-1499(2007)
AbstractThe 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.
Description7 pages, 3 figures.-- PMID: 18021750 [PubMed].-- PMCID: PMC2186377.-- Printed version published Dec 2007.-- Supplementary information (suppl. figure S1) available at the publisher website.
Publisher version (URL)http://dx.doi.org/10.1016/j.bbapap.2007.10.008
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