2ivv

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spinqualitylabelsall models 2ivv, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN COMPLEXED WITH THE INHIBITOR PP1

Overview

The RET proto-oncogene encodes a receptor tyrosine kinase for the glial, cell line-derived neurotrophic factor family of ligands. Loss-of-function, mutations in RET are implicated in Hirschsprung disease, whereas, activating mutations in RET are found in human cancers, including familial, medullar thyroid carcinoma and multiple endocrine neoplasias 2A and 2B. We, report here the biochemical characterization of the human RET tyrosine, kinase domain and the structure determination of the non-phosphorylated, and phosphorylated forms. Both structures adopt the same active kinase, conformation competent to bind ATP and substrate and have a pre-organized, activation loop conformation that is independent of phosphorylation, status. In agreement with the structural data, enzyme kinetic data show, ... [(full description)]

About this Structure

2IVV is a [Single protein] structure of sequence from [Homo sapiens] with PP1 and FMT as [ligands]. Active as [[1]], with EC number [2.7.10.1]. Full crystallographic information is available from [OCA].

Reference

Structure and chemical inhibition of the RET tyrosine kinase domain., Knowles PP, Murray-Rust J, Kjaer S, Scott RP, Hanrahan S, Santoro M, Ibanez CF, McDonald NQ, J Biol Chem. 2006 Nov 3;281(44):33577-87. Epub 2006 Aug 23. PMID:16928683

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