The crystal structure of a constitutively active mutant RON kinase suggests an intramolecular autophosphorylation hypothesis.

Article Details

Citation

Wang J, Steinbacher S, Augustin M, Schreiner P, Epstein D, Mulvihill MJ, Crew AP

The crystal structure of a constitutively active mutant RON kinase suggests an intramolecular autophosphorylation hypothesis.

Biochemistry. 2010 Sep 21;49(37):7972-4. doi: 10.1021/bi100409w.

PubMed ID
20726546 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Macrophage-stimulating protein receptorQ04912Details