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

Pub. Date : 2015 Nov

PMID : 26339056






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 STAT1 with excess amounts of Y3 was prone to inhibit the dephosphorylation at Tyr(701) by a phosphatase. Tyrosine signal transducer and activator of transcription 1 Homo sapiens
2 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 signal transducer and activator of transcription 1 Homo sapiens
3 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 signal transducer and activator of transcription 1 Homo sapiens
4 In virus-infected cells, phosphorylation of STAT1 at the Tyr(701) residue is potently enhanced, although transcription by STAT1 is inert. Tyrosine signal transducer and activator of transcription 1 Homo sapiens
5 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 signal transducer and activator of transcription 1 Homo sapiens