2h0q
From Proteopedia
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'''Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1)''' | '''Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1)''' | ||
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[[Category: Ford, B.]] | [[Category: Ford, B.]] | ||
[[Category: Nassar, N.]] | [[Category: Nassar, N.]] | ||
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:43:53 2008'' | |
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Revision as of 02:43, 4 May 2008
Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1)
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
2H0Q 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 Sun May 4 05:43:53 2008
Categories: Mus musculus | Single protein | Carpino, N. | Ford, B. | Nassar, N. | Pgm | Signaling protein | Sts-1