1oeo

From Proteopedia

Revision as of 16:13, 29 October 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1oeo, resolution 2.15Å

Drag the structure with the mouse to rotate

PTP1B WITH THE CATALYTIC CYSTEINE OXIDIZED TO SULFONIC ACID

Overview

The second messenger hydrogen peroxide is required for optimal activation, of numerous signal transduction pathways, particularly those mediated by, protein tyrosine kinases. One mechanism by which hydrogen peroxide, regulates cellular processes is the transient inhibition of protein, tyrosine phosphatases through the reversible oxidization of their, catalytic cysteine, which suppresses protein dephosphorylation. Here we, describe a structural analysis of the redox-dependent regulation of, protein tyrosine phosphatase 1B (PTP1B), which is reversibly inhibited by, oxidation after cells are stimulated with insulin and epidermal growth, factor. The sulphenic acid intermediate produced in response to PTP1B, oxidation is rapidly converted into a previously unknown sulphenyl-amide, species, in ... [(full description)]

About this Structure

1OEO is a [Single protein] structure of sequence from [Homo sapiens]. Active as [[1]], with EC number [3.1.3.48]. Full crystallographic information is available from [OCA].

Reference

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate., Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, Barford D, Nature. 2003 Jun 12;423(6941):769-73. PMID:12802338

Page seeded by OCA on Mon Oct 29 18:17:38 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools