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1oeo
From Proteopedia
(New page: 200px<br /> <applet load="1oeo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oeo, resolution 2.15Å" /> '''PTP1B WITH THE CATA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OEO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OEO OCA]]. | + | 1OEO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. 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]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OEO OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12802338 12802338] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12802338 12802338] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Andersen, J.N.]] | [[Category: Andersen, J.N.]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:43:38 2007'' |
Revision as of 09:38, 30 October 2007
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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 [Protein-tyrosine-phosphatase], with EC number [3.1.3.48]. Structure known Active Site: CAT. 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 Tue Oct 30 11:43:38 2007
