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1rpm
From Proteopedia
(New page: 200px<br /> <applet load="1rpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpm, resolution 2.3Å" /> '''HUMAN RECEPTOR PROTE...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1RPM 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=1RPM OCA]]. | + | 1RPM 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: ATE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RPM OCA]]. |
==Reference== | ==Reference== | ||
The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu., Hoffmann KM, Tonks NK, Barford D, J Biol Chem. 1997 Oct 31;272(44):27505-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9346878 9346878] | The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu., Hoffmann KM, Tonks NK, Barford D, J Biol Chem. 1997 Oct 31;272(44):27505-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9346878 9346878] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barford, D.]] | [[Category: Barford, D.]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''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 14:29:56 2007'' |
Revision as of 12:25, 30 October 2007
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HUMAN RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU, DOMAIN 1
Overview
Receptor-like protein-tyrosine phosphatases (RPTPs) play important roles, in regulating intracellular processes. We have been investigating the, regulation and function of RPTPmu, a receptor-like PTP related to the Ig, superfamily of cell adhesion molecules. Recently, the crystal structure of, a dimer of the membrane proximal domain of RPTPalpha (RPTPalpha D1) was, described (Bilwes, A. M., den Hertog, J., Hunter, T., and Noel J. P., (1996) Nature 382, 555-559). Within this crystal structure, the catalytic, site of each subunit of the dimer is sterically blocked by the insertion, of the N-terminal helix-turn-helix segment of the dyad-related monomer. It, was proposed that dimerization would lead to inhibition of catalytic, activity and may provide a paradigm for the regulation of the RPTP ... [(full description)]
About this Structure
1RPM 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: ATE. Full crystallographic information is available from [OCA].
Reference
The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu., Hoffmann KM, Tonks NK, Barford D, J Biol Chem. 1997 Oct 31;272(44):27505-8. PMID:9346878
Page seeded by OCA on Tue Oct 30 14:29:56 2007
