1yfo
From Proteopedia
(New page: 200px<br /> <applet load="1yfo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yfo, resolution 2.25Å" /> '''RECEPTOR PROTEIN TY...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1YFO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]]. 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=1YFO OCA]]. | + | 1YFO is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]]. 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 Sites: S1 and S2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YFO OCA]]. |
==Reference== | ==Reference== | ||
Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization., Bilwes AM, den Hertog J, Hunter T, Noel JP, Nature. 1996 Aug 8;382(6591):555-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8700232 8700232] | Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization., Bilwes AM, den Hertog J, Hunter T, Noel JP, Nature. 1996 Aug 8;382(6591):555-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8700232 8700232] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| + | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bilwes, A.M.]] | [[Category: Bilwes, A.M.]] | ||
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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 13:17:21 2007'' |
Revision as of 11:12, 30 October 2007
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RECEPTOR PROTEIN TYROSINE PHOSPHATASE ALPHA, DOMAIN 1 FROM MOUSE
Overview
Receptor-like protein-tyrosine phosphatases (RPTPs), like their, non-receptor counterparts, regulate the level of, phosphotyrosine-containing proteins derived from the action of, protein-tyrosine kinases. RPTPs are type-I integral membrane proteins, which contain one or two catalytic domains in their cytoplasmic region. It, is not known whether extracellular ligands regulate the activity of RPTPs., Here we describe the crystal structure of the membrane-proximal catalytic, domain (D1) of a typical RPTP, murine RPTP alpha. Significant structural, deviations from the PTP1B fold reside within the amino-terminal, helix-turn-helix segment of RPTPalphaD1 (residues 214 to 242) and a, distinctive two-stranded beta-sheet formed between residues 211-213 and, 458-461. The turn of the N-terminal ... [(full description)]
About this Structure
1YFO is a [Single protein] structure of sequence from [Mus musculus]. Active as [Protein-tyrosine-phosphatase], with EC number [3.1.3.48]. Structure known Active Sites: S1 and S2. Full crystallographic information is available from [OCA].
Reference
Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization., Bilwes AM, den Hertog J, Hunter T, Noel JP, Nature. 1996 Aug 8;382(6591):555-9. PMID:8700232
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