@text
 Tie2 (also known as Tek) is an endothelium-specific receptor tyrosine kinase involved in both angiogenesis and vasculature maintenance.  Vasculogenesis and angiogenesis are both important processes in embryonic development and several diseases such as ishemic coronary artery disease, cancer, diabetic retinopathy, and rheumatoid arthritis.  Normal vascular development depends on the function of endothelium-specific receptor tyrosine kinases such as Tie2.  Regulation of Tie2's kinas domain phosphorylation state and activity is important to vasculature development and maintenance.  Tie2 activity is regulated by agonistic and antagonistic extracellular ligands which prompt autophosphorylation (agonist) and inactivation (antagonist).  Mutations in Tie2 result in enhanced autophosphorylation and hereditary venous malformations.

The crystal structure of the Tie2 kinase domain has been determined to 2.2 A resolution.  The structure contains the catalytic core, the kinase insert domain (KID), and the C-terminal tail. The overall structure of Tie2K is analogous to structures reported for serine/threonine and tyrosine protein kinases.  Tie2K folds into two domains with the fold between the two domains being the catalytic site.  The N-terminal domain is responsible for ATP binding while the C-terminal domain is involved in catalysis and substrate binding.  The N-terminal domain folds into a twisted beta sheet and an alpha helix while the C-terminal domain contains seven alpha helices and two sets of anti-parallel beta strands. 

The length of the kinase insert domain may range from 12-97 residues.  This KID is thought to be important in protein-protein interactions involved in signaling thru autophosphorylation.  The C-terminal tail is shown to bind to several proteins containing src homology domain 2 and phosphotyrosine binding domains. It has also been shown that it must undergo a conformational change upon activation of a protein.

In addition to the domains mentioned above, there are also functionally important loop regions present in the crystal structure: the activation loop, the nucleotide binding loop, and the catalytic loop.  The activation loop is believed to regulate kinase activity.  In addition, its conformation is controlled by the phosphorylation of specific residues within that region.  The catalytic loop contains an aspatic acid that serves as the catalytic base in phosphotransfer reactions.  The nucleotide binding loop contains residues responsible for binding the triphosphate moiety of ATP in the correct position for catalysis.  ATP has not been successfully crystallized with the structure.    

Reference:
Shewchuk,L.M., Hassell,A.M., Ellis,B., Holmes,W.D., Davis,R., Horne,E.L., Kadwell,S.H., Mckee,D.D., Moore,J.T.(2000).  Structure of the Tie2 RTK Domain:  Self-Inhibition by the Nucleotide Binding Loop, Activation Loop, and C-Terminal Tail. Structure 8,1105-1113.
@kinemageTie2 
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Tie2 Kinase Domain

The crystal structure has been determined to 2.2 A.  The catalytic loop (red) contains an aspartic acid (gray) that serves as the catalytic base in phosphotransfer reactions. The kinase insert domain (KID)(magenta) comprises two short helical segments that pack against the C-terminal lobe and tail. The Tie2K nucleotide binding loop (blue) is in an inhibitory conformation.  Its activation loop (cyan) adopts an activated-like conformation in the absence of phosphorylation. Tyr-897 (green), located in the N-terminal domain, may negatively regulate the activity of Tie2 by preventing dimerization of the kinase domains or by recruiting phosphatases when it is phosphorylated.   Conformational changes in the nucleotide binding loop, activation loop, C helix, and the C-terminal tail are required for ATP and substrate binding.  Six residues at the N-terminus, three residues at the C-terminus, four residues in the activation loop, and six residues connecting beta3 and alphaC were disordered and are not present in the crystal structure.

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