Title : Structural basis for the regulatory role of the PPxY motifs in the thioredoxin-interacting protein TXNIP.

Pub. Date : 2016 Jan 15

PMID : 26527736






2 Functional Relationships(s)
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1 Phosphorylation of this tyrosine residue of TXNIP diminished the binding capability of PPxY motifs of TXNIP to Itch, whereas this phosphorylation is a prerequisite to the binding activity of TXNIP to SHP2 [SH2 (Src homology 2) domain-containing protein tyrosine phosphatase 2] and their roles in stabilizing the phosphorylation and activation of CSK (c-Src tyrosine kinase). Tyrosine C-terminal Src kinase Homo sapiens
2 Phosphorylation of this tyrosine residue of TXNIP diminished the binding capability of PPxY motifs of TXNIP to Itch, whereas this phosphorylation is a prerequisite to the binding activity of TXNIP to SHP2 [SH2 (Src homology 2) domain-containing protein tyrosine phosphatase 2] and their roles in stabilizing the phosphorylation and activation of CSK (c-Src tyrosine kinase). Tyrosine C-terminal Src kinase Homo sapiens