Title : Mutations in the linker domain affect phospho-STAT3 function and suggest targets for interrupting STAT3 activity.

Pub. Date : 2015 Dec 1

PMID : 26553978






2 Functional Relationships(s)
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1 Crystallography of the cores of phosphotyrosine-activated dimers of STAT1 (132-713) and STAT3 (127-722) bound to a similar double-stranded deoxyoligonucleotide established the domain structure of the STATs and the structural basis for activation through tyrosine phosphorylation and dimerization. Tyrosine signal transducer and activator of transcription 1 Homo sapiens
2 Crystallography of the cores of phosphotyrosine-activated dimers of STAT1 (132-713) and STAT3 (127-722) bound to a similar double-stranded deoxyoligonucleotide established the domain structure of the STATs and the structural basis for activation through tyrosine phosphorylation and dimerization. Tyrosine signal transducer and activator of transcription 1 Homo sapiens