Transferase(Phosphotransferase); domain 1
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
Identification of anaplastic lymphoma kinase as a receptor for the growth factor pleiotrophin.
Midkine binds to anaplastic lymphoma kinase (ALK) and acts as a growth factor for different cell types.
Unique substrate specificity of anaplastic lymphoma kinase (ALK): development of phosphoacceptor peptides for the assay of ALK activity.
Characterization of some molecular mechanisms governing autoactivation of the catalytic domain of the anaplastic lymphoma kinase.
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1072-1410.
Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain.
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1094-1407 IN COMPLEX WITH INHIBITOR.
Crystal structures of anaplastic lymphoma kinase in complex with ATP competitive inhibitors.
Structural basis for the recognition of nucleophosmin-anaplastic lymphoma kinase oncoprotein by the phosphotyrosine binding domain of Suc1-associated neurotrophic factor-induced tyrosine-phosphorylated target-2.
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1069-1411 IN COMPLEX WITH INHIBITOR, ENZYME REGULATION.
CH5424802, a selective ALK inhibitor capable of blocking the resistant gatekeeper mutant.
Structure Based Drug Design of Crizotinib (PF-02341066), a Potent and Selective Dual Inhibitor of Mesenchymal-Epithelial Transition Factor (c-MET) Kinase and Anaplastic Lymphoma Kinase (ALK).
Rapid development of piperidine carboxamides as potent and selective anaplastic lymphoma kinase inhibitors.
The discovery and optimization of a novel class of potent, selective, and orally bioavailable anaplastic lymphoma kinase (ALK) inhibitors with potential utility for the treatment of cancer.
The R1275Q neuroblastoma mutant and certain ATP-competitive inhibitors stabilize alternative activation loop conformations of anaplastic lymphoma kinase.
This enzyme is a receptor for growth factors, pleiotrophin (UniProt; P21246) and midkine (UniProt; P21741), which are homologous to each other (see [1] and [2]). This enzyme belongs to the insulin receptor kinase superfamily (see [5]). This enzyme consists of the N-terminal extracellular region, the transmembrane region and the C-terminal cytoplasmic region (see [5]). The extracellular region is composed of an N-terminal region, whose structure has not been elucidated yet, two MAM domains, low-density lipoprotein class A (LDL-A) domain, and a glycine-rich region (see [5]). The cytoplasmic region is composed of a juxtamembrane region, a catalytic domain and a C-terminal region (see [5]). The catalytic domain is homologous to that of insulin receptor kinase (M00129 in EzCatDB).