ArticleBiochimica et biophysica acta2007
3D structure of Syk kinase determined by single-particle electron microscopy.
Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Platelet Membrane Receptors and Signalling Pathways.Handbook of experimental pharmacology · 2026Review
- Entropic allostery dominates the phosphorylation-dependent regulation of Syk tyrosine kinase release from immunoreceptor tyrosine-based activation motifs.Protein science : a publication of the Protein Society · 2018Article
- Phosphorylation impact on Spleen Tyrosine kinase conformation by Surface Enhanced Raman Spectroscopy.Scientific reports · 2017Article
- Biophysical and mechanistic insights into novel allosteric inhibitor of spleen tyrosine kinase.The Journal of biological chemistry · 2012Article
- Engineered nanostructures of antigen provide an effective means for regulating mast cell activation.ACS nano · 2011Article
- Article
- The SYK tyrosine kinase: a crucial player in diverse biological functions.Nature reviews. Immunology · 2010Review
- Conformational rearrangements upon Syk auto-phosphorylation.Biochimica et biophysica acta · 2009Article
- Syk and pTyr'd: Signaling through the B cell antigen receptor.Biochimica et biophysica acta · 2009Review
- The tyrosine kinase network regulating mast cell activation.Immunological reviews · 2009Review
- Differential dephosphorylation of the FcRgamma immunoreceptor tyrosine-based activation motif tyrosines with dissimilar potential for activating Syk.The Journal of biological chemistry · 2008Article
- Image processing for electron microscopy single-particle analysis using XMIPP.Nature protocols · 2008Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.