1oet: Difference between revisions

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[[Image:1oet.jpg|left|200px]]<br /><applet load="1oet" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1oet.jpg|left|200px]]
caption="1oet, resolution 2.30&Aring;" />
 
'''OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B'''<br />
{{Structure
|PDB= 1oet |SIZE=350|CAPTION= <scene name='initialview01'>1oet</scene>, resolution 2.30&Aring;
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''OXIDATION STATE OF PROTEIN TYROSINE PHOSPHATASE 1B'''
 


==Overview==
==Overview==
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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 <scene name='pdbligand=MG:'>MG</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1OET OCA].  
1OET is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OET OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12802339 12802339]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12802339 12802339]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]
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[[Category: protein tyrosine phosphatase]]
[[Category: protein tyrosine phosphatase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:56 2008''
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Revision as of 14:09, 20 March 2008

File:1oet.jpg


PDB ID 1oet

Drag the structure with the mouse to rotate
, resolution 2.30Å
Sites:
Ligands:
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Coordinates: save as pdb, mmCIF, xml



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. 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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