2ikq
From Proteopedia
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| - | [[Image:2ikq.jpg|left|200px]] | + | [[Image:2ikq.jpg|left|200px]] |
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| - | '''Crystal structure of mouse Sts-1 PGM domain in complex with phosphate''' | + | {{Structure |
| + | |PDB= 2ikq |SIZE=350|CAPTION= <scene name='initialview01'>2ikq</scene>, resolution 2.609Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= Sts-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of mouse Sts-1 PGM domain in complex with phosphate''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IKQ is a [ | + | 2IKQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IKQ OCA]. |
==Reference== | ==Reference== | ||
| - | A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling., Mikhailik A, Ford B, Keller J, Chen Y, Nassar N, Carpino N, Mol Cell. 2007 Aug 3;27(3):486-97. PMID:[http:// | + | A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling., Mikhailik A, Ford B, Keller J, Chen Y, Nassar N, Carpino N, Mol Cell. 2007 Aug 3;27(3):486-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17679096 17679096] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''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 17:30:43 2008'' |
Revision as of 15:30, 20 March 2008
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| , resolution 2.609Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Sts-1 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of mouse Sts-1 PGM domain in complex with phosphate
Overview
Precise signaling by the T cell receptor (TCR) is crucial for a proper immune response. To ensure that T cells respond appropriately to antigenic stimuli, TCR signaling pathways are subject to multiple levels of regulation. Sts-1 negatively regulates signaling pathways downstream of the TCR by an unknown mechanism(s). Here, we demonstrate that Sts-1 is a phosphatase that can target the tyrosine kinase Zap-70 among other proteins. The X-ray structure of the Sts-1 C terminus reveals that it has homology to members of the phosphoglycerate mutase/acid phosphatase (PGM/AcP) family of enzymes, with residues known to be important for PGM/AcP catalytic activity conserved in nature and position in Sts-1. Point mutations that impair Sts-1 phosphatase activity in vitro also impair the ability of Sts-1 to regulate TCR signaling in T cells. These observations reveal a PGM/AcP-like enzyme activity involved in the control of antigen receptor signaling.
About this Structure
2IKQ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling., Mikhailik A, Ford B, Keller J, Chen Y, Nassar N, Carpino N, Mol Cell. 2007 Aug 3;27(3):486-97. PMID:17679096
Page seeded by OCA on Thu Mar 20 17:30:43 2008
