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Switch #:
SWTI000346
Switch type:
Avidity-sensing

Description:
Phosphorylation of Y188 and Y199 in the ITAM motif of T-cell surface glycoprotein CD3 epsilon chain (CD3E) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase SYK (SYK).

Participants:
(1) T-cell surface glycoprotein CD3 epsilon chain (CD3E)
(2) Tyrosine-protein kinase SYK (SYK)

Interactions
Interaction #1 CD3E - SYK

Interfaces
(1) LIG_TYR_ITAM motif (185NPDYEPIRKGQRDLYSGL202) in T-cell surface glycoprotein CD3 epsilon chain (CD3E)
(2) SH2 domain (15-92) in Tyrosine-protein kinase SYK (SYK)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of Y188 and Y199 on T-cell surface glycoprotein CD3 epsilon chain (CD3E)) of the T-cell surface glycoprotein CD3 epsilon chain (CD3E) LIG_TYR_ITAM motif - Tyrosine-protein kinase SYK (SYK) SH2 domain interaction


Additional Information
Structural information: 1A81
Interaction #2 CD3E - SYK

Interfaces
(3) LIG_TYR_ITAM motif (185NPDYEPIRKGQRDLYSGL202) in T-cell surface glycoprotein CD3 epsilon chain (CD3E)
(4) SH2 domain (168-244) in Tyrosine-protein kinase SYK (SYK)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of Y188 and Y199 on T-cell surface glycoprotein CD3 epsilon chain (CD3E)) of the T-cell surface glycoprotein CD3 epsilon chain (CD3E) LIG_TYR_ITAM motif - Tyrosine-protein kinase SYK (SYK) SH2 domain interaction


Additional Information
Structural information: 1A81
Context
References

(1) Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide.
F├╝tterer et al. J. Mol. Biol. (1998)

See also

Other switches involving participants
T-cell surface glycoprotein CD3 epsilon chain (CD3E) - 2 more (view)
Tyrosine-protein kinase SYK (SYK) - 4 more (view)

Other switches involving interfaces
SH2 domain - 140 more (view)
LIG_TYR_ITAM - 8 more (view)




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