Switch #:
SWTI000344
Switch type:
Avidity-sensing

Description:
Phosphorylation of Y72 and Y83 in the ITAM motif of T-cell surface glycoprotein CD3 zeta chain (CD247) induces high-avidity binding to the tandem SH2 domains of Tyrosine-protein kinase ZAP-70 (ZAP70).

Participants:
(1) T-cell surface glycoprotein CD3 zeta chain (CD247)
(2) Tyrosine-protein kinase ZAP-70 (ZAP70)

Interactions
Interaction #1 CD247 - ZAP70

Interfaces
(1) LIG_TYR_ITAM motif (69NQLYNELNLGRREEYDVL86) in T-cell surface glycoprotein CD3 zeta chain (CD247)
(2) SH2 domain (10-87) in Tyrosine-protein kinase ZAP-70 (ZAP70)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of Y72 and Y83 on T-cell surface glycoprotein CD3 zeta chain (CD247)) of the T-cell surface glycoprotein CD3 zeta chain (CD247) LIG_TYR_ITAM motif - Tyrosine-protein kinase ZAP-70 (ZAP70) SH2 domain interaction

Additional Information
Affinity : N-SH2 + C-SH2: 0.0214 µM, N-SH2: 1.8 µM, C-SH2: 3.5 µM
Interaction #2 CD247 - ZAP70

Interfaces
(3) LIG_TYR_ITAM motif (69NQLYNELNLGRREEYDVL86) in T-cell surface glycoprotein CD3 zeta chain (CD247)
(4) SH2 domain (163-239) in Tyrosine-protein kinase ZAP-70 (ZAP70)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of Y72 and Y83 on T-cell surface glycoprotein CD3 zeta chain (CD247)) of the T-cell surface glycoprotein CD3 zeta chain (CD247) LIG_TYR_ITAM motif - Tyrosine-protein kinase ZAP-70 (ZAP70) SH2 domain interaction

Additional Information
Affinity : N-SH2 + C-SH2: 0.0214 µM, N-SH2: 1.8 µM, C-SH2: 3.5 µM
Context
References

(1) Analysis of the interaction of ZAP-70 and syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance.
Bu et al. Proc. Natl. Acad. Sci. U.S.A. (1995)

(2) Functional analysis of immunoreceptor tyrosine-based activation motif (ITAM)-mediated signal transduction: the two YxxL segments within a single CD3zeta-ITAM are functionally distinct.
Sunder-Plassmann et al. Eur. J. Immunol. (1997)




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