TY - JOUR
T1 - 3D structure of Syk kinase determined by single-particle electron microscopy
AU - Arias-Palomo, Ernesto
AU - Recuero-Checa, María A.
AU - Bustelo, Xosé R.
AU - Llorca, Oscar
N1 - Funding Information:
OL's work is supported by grants SAF2005-00775 (OL) and GEN2003-20239-C06-06 from the Spanish Ministry of Education and Science (MES). XRB's work is supported by grants from the US National Cancer Institute (5R01-CA73735-10), the MES (SAF2006-01789 and GEN2003-20239-C06-01), and the Red Temática de Investigación Cooperativa en Cáncer (RD06/0020/0001, Spanish Ministry of Health). All Spanish funding is co-sponsored by the European FEDER program.
PY - 2007/12
Y1 - 2007/12
N2 - 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.
AB - 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.
KW - EM
KW - Kinases
KW - Single-particle electron microscopy
KW - Syk
KW - Zap-70
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U2 - 10.1016/j.bbapap.2007.10.008
DO - 10.1016/j.bbapap.2007.10.008
M3 - Article
C2 - 18021750
AN - SCOPUS:36849022556
SN - 1570-9639
VL - 1774
SP - 1493
EP - 1499
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 12
ER -