Transferase(Phosphotransferase); domain 1
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
insulin receptor protein-tyrosine kinase
Self-association studies on the EphB2 receptor SAM domain using analytical ultracentrifugation.
Olfactory marker protein (OMP) exhibits a beta-clam fold in solution: implications for target peptide interaction and olfactory signal transduction.
Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells.
Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2.
PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands.
Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region.
alphaPIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase.
Isolation and characterization of Dek, a Drosophila eph receptor protein tyrosine kinase.
Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain.
The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization.
Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites.
Oligomeric structure of the human EphB2 receptor SAM domain.
Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors.
Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons.
Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region.
Crystal structure of an Eph receptor-ephrin complex.
The crystal structure of the olfactory marker protein at 2.3 A resolution.
The role of the Eph-ephrin signalling system in the regulation of developmental patterning.
Regulation and targets of receptor tyrosine kinases.
Eph family functions from an evolutionary perspective.
The E.C. was transferred from 2.7.1.112 to 2.7.10.1. The Eph receptor tyrosine kinase family is regulated by autophosphorylation within the juxtamembrane region and the kinase activation segment. This receptor enzyme has N-terminal extracellular region, which is composed of ligand-binding domain, Cys-rich domain, and two fibronectine type-III domain, transmembrane region, and cytoplasmic region, which is composed of juxtamembrane region, protein kinase domain, and SAM domain. PDB structures, 1nuk & 1kgy, correspond to the first domain of this enzyme, ligand-binding domain, the other structure, 1jpa, comprises the fifth domain, juxtamembrane region, and the sixth domain, protein kinase domain. PDB structure, 1sgg, corresponds to the last domain, SAM. However, tertiary structures of the rest of domains, the second domain, Cys-rich domain, the third and fourth domains, two fibronectin type-III domains, have not been determined yet. The last domain is sterile alpha motif (SAM) domain, which was found in various signaling proteins such as tyrosine and serine/threonine protein kinases, regulators of lipid metabolism, and GTPases, according to the literature [9]. The SAM domain is involved in protein-protein interaction, rather than catalysis, through the ability to oligomerize with other SAM domains [9]. This SAM domain has a conserved tyrosine (Tyr25, PDB;1sgg), which was reported to be essential for the interaction with SH2 domains after its phosphorylation (see paper [10]). Although the tertiary structure of the catalytic domain has been determined, its catalytic mechanism is still unclear. However, since the structure is homologous to other kinase domains with complete conservation of active site residues, the mechanism can be similar to those ones (see M00129).