Active JAK kinase phosphorylates several tyrosine residues in the receptor’s cytosolic domain and activates a STAT transcription factor that moves directly to the nucleus

TLS Online TPP Program

#Id: 9609

#XL - T Zoology

Phosphorylation leads to a conformational change in the activation loop that unblocks kinase active site by reducing the Kd for ATP or the substrate to be phosphorylated.

TLS Online TPP Program

#Id: 9610

#XL - T Zoology

Insulin receptor, form disulfide-linked dimers in the absence of hormone.

TLS Online TPP Program

#Id: 9611

#XL - T Zoology

Binding of ligand to predimerized but inactive RTK alters the conformation of the dimer in such a way that the receptor’s kinase becomes activated.

TLS Online TPP Program

#Id: 9612

#XL - T Zoology

TLS Online TPP Program

#Id: 9613

#XL - T Zoology

In the absence of insulin, the extracellular domain adopts a symmetric inverted U-shaped conformation. 

TLS Online TPP Program

#Id: 9614

#XL - T Zoology

Upon insulin binding, the extracellular domain is converted into a T-shaped conformation that brings the transmembrane domains together.