Transferase(Phosphotransferase); domain 1
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF.
Characterization of a multicomponent receptor for GDNF.
A GPI-linked protein that interacts with Ret to form a candidate neurturin receptor.
Calcium-dependent Ret activation by GDNF and neurturin.
Distinct structural elements in GDNF mediate binding to GFRalpha1 and activation of the GFRalpha1-c-Ret receptor complex.
Molecular modeling of the extracellular domain of the RET receptor tyrosine kinase reveals multiple cadherin-like domains and a calcium-binding site.
The GDNF family: signalling, biological functions and therapeutic value.
Identification of a surface for binding to the GDNF-GFR alpha 1 complex in the first cadherin-like domain of RET.
The structure of GFRalpha1 domain 3 reveals new insights into GDNF binding and RET activation.
Direct interactions among Ret, GDNF and GFRalpha1 molecules reveal new insights into the assembly of a functional three-protein complex.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 705-1013 ALONE AND IN COMPLEX WITH INHIBITORS, MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-900 AND TYR-905.
Structure and chemical inhibition of the RET tyrosine kinase domain.
Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret.
Structure of artemin complexed with its receptor GFRalpha3: convergent recognition of glial cell line-derived neurotrophic factors.
GDNF family receptor complexes are emerging drug targets.
The structure of the glial cell line-derived neurotrophic factor-coreceptor complex: insights into RET signaling and heparin binding.
Synthesis, structure-activity relationship and crystallographic studies of 3-substituted indolin-2-one RET inhibitors.
Mammal-restricted elements predispose human RET to folding impairment by HSCR mutations.
This enzyme belongs to receptor tyrosine kinase family. This enzyme consists of the N-terminal extracellular region, the transmembrane region, and the C-terminal intracellular region (see [7] and [11]). The extracellular region is composed of four N-terminal cadherin-like domains followed by a cysteine-rich domain (see [6], [7] and [11]). On the other hand, the intracellular region is composed of a juxtamembrane domain, a kinase domain, and a tail region (see [7] and [11]). The catalytic domain of this enzyme is homologous to that of vascular endothelial growth factor receptor (M00131 in EzCatDB). According to the literature [7], [8], [10] and [11], this enzyme is activated by binding to a complex of a glial cell line-derived neutrophic factor (GDNF) family ligand and its cognate receptor, the GDNF family receptor alpha (GFRalpha). The GDNF family ligands, including GDNF, neurturin (NRTN), artemin (ARTN) and persephin (PSPN), are homologous to the transforming growth factor-beta (TGF-beta) (see [7]). GFRalpha1 binds preferentially to GDNF, GFRalpha2 to NRTN, GFRalpha3 to ARTN, and GFRalpha4 to PSPN (see [7] and [13]). These receptor complexes with this enzyme can be drug targets (see [14]). According to the literature[11], autophosphorylation of Tyr905 on A-loop is not required for RET catalytic activity.