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1fpr

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[[Image:1fpr.jpg|left|200px]]
[[Image:1fpr.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1fpr |SIZE=350|CAPTION= <scene name='initialview01'>1fpr</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1fpr", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene>
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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_1fpr| PDB=1fpr | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpr OCA], [http://www.ebi.ac.uk/pdbsum/1fpr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fpr RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.'''
'''CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.'''
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[[Category: Zhao, Z J.]]
[[Category: Zhao, Z J.]]
[[Category: Zhou, G W.]]
[[Category: Zhou, G W.]]
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[[Category: protein tyrosine phosphatase]]
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[[Category: Protein tyrosine phosphatase]]
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[[Category: residue shift]]
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[[Category: Residue shift]]
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[[Category: substrate specificity]]
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[[Category: Substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:37:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:27:46 2008''
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Revision as of 13:37, 2 May 2008

Template:STRUCTURE 1fpr

CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.


Overview

The substrate specificity of the catalytic domain of SHP-1, an important regulator in the proliferation and development of hematopoietic cells, is critical for understanding the physiological functions of SHP-1. Here we report the crystal structures of the catalytic domain of SHP-1 complexed with two peptide substrates derived from SIRPalpha, a member of the signal-regulatory proteins. We show that the variable beta5-loop-beta6 motif confers SHP-1 substrate specificity at the P-4 and further N-terminal subpockets. We also observe a novel residue shift at P-2, the highly conserved subpocket in protein- tyrosine phosphatases. Our observations provide new insight into the substrate specificity of SHP-1.

About this Structure

1FPR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1., Yang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW, J Biol Chem. 2000 Feb 11;275(6):4066-71. PMID:10660565 Page seeded by OCA on Fri May 2 16:37:10 2008

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