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

Ernesto Arias-Palomo, María A. Recuero-Checa, Xosé R. Bustelo, Oscar Llorca

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1493-1499
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number12
StatePublished - Dec 2007
Externally publishedYes


  • EM
  • Kinases
  • Single-particle electron microscopy
  • Syk
  • Zap-70

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology


Dive into the research topics of '3D structure of Syk kinase determined by single-particle electron microscopy'. Together they form a unique fingerprint.

Cite this