Title : Structural Basis of the Inhibition of STAT1 Activity by Sendai Virus C Protein.

Pub. Date : 2015 Nov

PMID : 26339056






2 Functional Relationships(s)
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Protein Name
Organism
1 In an electrophoretic mobility shift assay, tyrosine-phosphorylated STAT1 (pY-STAT1) with Y3 associated with the gamma-activated sequence, probably as high-molecular-weight complexes (HMWCs), which may account for partial inhibition of a reporter assay from IFN-gamma by Y3. Tyrosine interferon gamma Homo sapiens
2 Molecular modeling and experiments suggested that the two C proteins bind to and stabilize the parallel form of the STAT1 dimer, which are likely to be phosphorylated at Tyr(701), further inducing high-molecular-weight complex formation and inhibition of transcription by IFN-gamma. Tyrosine interferon gamma Homo sapiens