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Details on Person Receptor tyrosine kinase activation and signaling are typica...
| Class:Id | Summation:210873 |
|---|---|
| _displayName | Receptor tyrosine kinase activation and signaling are typica... |
| _timestamp | 2008-02-05 13:52:39 |
| created | [InstanceEdit:210879] Garapati, P V, 2008-01-17 14:13:36 |
| literatureReference | [LiteratureReference:210860] Structure of the Tie2 RTK domain: self-inhibition by the nucleotide binding loop, activation loop, and C-terminal tail |
| modified | [InstanceEdit:211548] Garapati, P V, 2008-02-05 13:52:09 |
| text | Receptor tyrosine kinase activation and signaling are typically initiated via dimerization of the receptors through homo-oligomeric ligand binding. Angiopoietin1 may form homotrimers, but in most cases it assembles into higher-order multimers. This oligomerization is mediated by the N-ter coiled coil domain (CCD). The binding of Ang1 oligomers to Tie2 promotes the dimerization of Tie2, which is further assisted by the interaction between the kinase domains of the receptors. |
| (summation) | [Reaction:210881] Dimerization of Tie2/Ang1 complex [Homo sapiens] |
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No pathways have been reviewed or authored by Receptor tyrosine kinase activation and signaling are typica... (210873)
