Stability of an autoinhibitory interface in the structure of the tyrosine kinase ZAP-70 impacts T cell receptor response.
AuthorsDeindl S, Kadlecek TA, Cao X, Kuriyan J, Weiss A,
JournalProc Natl Acad Sci U S A
PubMed ID19920178
'The delivery of signals from the activated T cell antigen receptor (TCR) inside the cell relies on the protein tyrosine kinase ZAP-70 (zeta-associated protein of 70 kDa). A recent crystal structure of inactive full-length ZAP-70 suggests that a central interface formed by the docking of the two SH2 domains of ... More
Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases.
AuthorsBrdicka T, Kadlecek TA, Roose JP, Pastuszak AW, Weiss A,
JournalMol Cell Biol
PubMed ID15923611
ZAP-70, a Syk family cytoplasmic protein tyrosine kinase (PTK), is required to couple the activated T-cell antigen receptor (TCR) to downstream signaling pathways. It contains two tandem SH2 domains that bind to phosphorylated TCR subunits and a C-terminal catalytic domain. The region connecting the SH2 domains with the kinase domain, ... More