Sandbox Reserved 1490: Difference between revisions
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{{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_ESBS}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Crystal structure of cytoplasmic kinase domain of Tie2 in complex with decipera compound DP1919== | ==Crystal structure of cytoplasmic kinase domain of Tie2 in complex with decipera compound DP1919== | ||
< | <StructureSection load='6mwe' size='340' side='right' caption='Structure of the kinase domain of TIE2.' scene=''/> | ||
The protein we are focusing one is a protein kinase receptor to a family of ligands called angiopoietins. This receptor is a Tyrosine Kinase TIE2. We are going to analyze the <scene name='80/802664/Entire_molecule/1'>kinase domain</scene> of this protein. | The protein we are focusing one is a protein kinase receptor to a family of ligands called angiopoietins. This receptor is a Tyrosine Kinase TIE2. We are going to analyze the <scene name='80/802664/Entire_molecule/1'>kinase domain</scene> of this protein. | ||
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While ANGPT1 is a TIE2 agonist and has a higher binding affinity to it than ANGPT2, ANGPT2 can act as a context-dependent agonist. Thus, the ANGPT/TIE2 kinase signaling pathway is an attractive anti-vascular target. | While ANGPT1 is a TIE2 agonist and has a higher binding affinity to it than ANGPT2, ANGPT2 can act as a context-dependent agonist. Thus, the ANGPT/TIE2 kinase signaling pathway is an attractive anti-vascular target. | ||
== Function == | == Function == | ||
