title: The crystal structure of a constitutively active mutant RON kinase suggests an intramolecular autophosphorylation hypothesis.
abstract: A complex of RON(M1254T) with AMP-PNP and Mg(2+) reveals a substratelike positioning of Tyr1238 as well as likely catalysis-competent placement of the AMP-PNP and Mg(2+) components and indicates a tendency for cis phosphorylation. The structure shows how the oncogenic mutation may cause the constitutive activation and suggests a mechanistic hypothesis for the autophosphorylation of receptor tyrosine kinases.
authors: OSI Pharmaceuticals, Inc., 1 Bioscience Park Drive, Farmingdale, New York 11735, USA. jwang@osip.com
authors: Jing
authors: J
authors: Wang
authors: Stefan
authors: S
authors: Steinbacher
authors: Martin
authors: M
authors: Augustin
authors: Patrick
authors: P
authors: Schreiner
authors: David
authors: D
authors: Epstein
authors: Mark J
authors: MJ
authors: Mulvihill
authors: Andrew P
authors: AP
authors: Crew
mesh_terms: D000266:Adenylyl Imidodiphosphate; D010766:Phosphorylation; D010770:Phosphotransferases; D020794:Receptor Protein-Tyrosine Kinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D000266:Adenylyl Imidodiphosphate; D010770:Phosphotransferases; D020794:Receptor Protein-Tyrosine Kinases