1fpr
From Proteopedia
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| - | [[Image:1fpr.jpg|left|200px]] | + | [[Image:1fpr.jpg|left|200px]] |
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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.''' | + | {{Structure |
| + | |PDB= 1fpr |SIZE=350|CAPTION= <scene name='initialview01'>1fpr</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''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== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FPR is a [ | + | 1FPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FPR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10660565 10660565] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
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[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:22 2008'' |
Revision as of 09:12, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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