1oet: Difference between revisions
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[[Image:1oet. | [[Image:1oet.jpg|left|200px]]<br /><applet load="1oet" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1oet" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1oet, resolution 2.30Å" /> | caption="1oet, resolution 2.30Å" /> | ||
'''OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B'''<br /> | '''OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] | 1OET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OET OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: protein tyrosine phosphatase]] | [[Category: protein tyrosine phosphatase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:39:06 2007'' | ||
Revision as of 18:29, 18 December 2007
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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 target in type II diabetes and obesity. We also identify a, sulphenyl-amide species that is formed through oxidation of its catalytic, cysteine. Formation of the sulphenyl-amide causes large changes in the, PTP1B active site, which are reversible by reduction with the cellular, reducing agent glutathione. The sulphenyl-amide is a protective, intermediate in the oxidative inhibition of PTP1B. In addition, it may, facilitate reactivation of PTP1B by biological thiols and signal a unique, state of the protein.
DiseaseDisease
Known diseases associated with this structure: Abdominal body fat distribution, modifier of OMIM:[176885], Insulin resistance, susceptibility to OMIM:[176885]
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 Known structural/functional Site: . 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
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