All RTKs have a cytosolic domain with protein tyrosine kinase activity

TLS Online TPP Program

#Id: 9643

#XL - T Zoology

Molecular Handcuff 

Phosphorylation of Raf is recognize by protein 14-3-3 dimer, which locks the autoinhibitory domain in a position where it blocks and inhibits the kinase active site

TLS Online TPP Program

#Id: 9644

#XL - T Zoology

TLS Online TPP Program

#Id: 9645

#XL - T Zoology

Active Ras⋅GTP binds to the N-terminal autoinhibitory domain of Raf, altering its conformation and allowing the phosphate attached to this domain to be removed by cytosolic phosphatases, causing loss of 14-3-3 binding.

TLS Online TPP Program

#Id: 9646

#XL - T Zoology

Active Raf phosphorylates MEK on one or two serine residues in its activation loop, activating MEK kinase activity

TLS Online TPP Program

#Id: 9647

#XL - T Zoology

Constitutively active Raf kinase

a glutamic acid substitution for the valine at position 600

TLS Online TPP Program

#Id: 9648

#XL - T Zoology

MEK is a dual-specificity protein kinase

phosphorylates its target proteins on both tyrosine and serine/threonine