1yfo

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[[Image:1yfo.gif|left|200px]]
[[Image:1yfo.gif|left|200px]]
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{{Structure
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|PDB= 1yfo |SIZE=350|CAPTION= <scene name='initialview01'>1yfo</scene>, resolution 2.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1yfo", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=S1:Active+Site'>S1</scene> and <scene name='pdbsite=S2:Active+Site'>S2</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1yfo| PDB=1yfo | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfo OCA], [http://www.ebi.ac.uk/pdbsum/1yfo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yfo RCSB]</span>
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}}
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'''RECEPTOR PROTEIN TYROSINE PHOSPHATASE ALPHA, DOMAIN 1 FROM MOUSE'''
'''RECEPTOR PROTEIN TYROSINE PHOSPHATASE ALPHA, DOMAIN 1 FROM MOUSE'''
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[[Category: Bilwes, A M.]]
[[Category: Bilwes, A M.]]
[[Category: Noel, J P.]]
[[Category: Noel, J P.]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: receptor]]
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[[Category: Receptor]]
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[[Category: signal]]
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[[Category: Signal]]
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[[Category: signal transduction]]
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[[Category: Signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:15:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:05:49 2008''
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Revision as of 13:15, 3 May 2008

Image:1yfo.gif

Template:STRUCTURE 1yfo

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 segment inserts into the active site of a dyad-related D1 monomer. On the basis of two independent crystal structures, sequence alignments, and the reported biological activity of EGF receptor/CD45 chimaeras, we propose that dimerization and active-site blockage is a physiologically important mechanism for downregulating the catalytic activity of RPTPalpha and other RPTPs.

About this Structure

1YFO is a Single protein structure of sequence from Mus musculus. 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 Page seeded by OCA on Sat May 3 16:15:49 2008

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