Báo cáo khoa học: Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein
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TheB class cell-attachedephrinsmediate contact-dependentcell–cell communications and transduce the contact signalsto the host cells through the binding interactions of theircytoplasmic domains. Two classes of intracellular effectorsof B ephrins have been identified: one contains the PSD-95/Dlg/ZO-1 (PDZ)domain(for examplePDZ-RGS3), and thesecond the Src homology 2 (SH2) domain (e.g. the Grb4adaptor protein). The interaction with Grb4 requires phos-phorylation of tyrosine residues on the conserved cytoplas-mic C-terminal region of B ephrins, while binding to thePDZ domain is independent of tyrosine phosphorylation....
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Báo cáo khoa học: Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein
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