1oet
|
OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B
OverviewOverview
Protein tyrosine phosphatases regulate signal transduction pathways, involving tyrosine phosphorylation and have been implicated in the, development of cancer, diabetes, rheumatoid arthritis and hypertension., Increasing evidence suggests that the cellular redox state is involved in, regulating tyrosine phosphatase activity through the reversible, oxidization of the catalytic cysteine to sulphenic acid (Cys-SOH). But how, further oxidation to the irreversible sulphinic (Cys-SO2H) and sulphonic, (Cys-SO3H) forms is prevented remains unclear. Here we report the crystal, structures of the regulatory sulphenic and irreversible sulphinic and, sulphonic acids of protein tyrosine phosphatase 1B (PTP1B), an important, enzyme in the negative regulation of the insulin receptor and a, therapeutic ... [(full description)]
About this StructureAbout this Structure
1OET is a [Single protein] structure of sequence from [Homo sapiens] with MG as [ligand]. Active as [Protein-tyrosine-phosphatase], with EC number [3.1.3.48]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B., van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H, Nature. 2003 Jun 12;423(6941):773-7. PMID:12802339
Page seeded by OCA on Tue Oct 30 15:51:48 2007