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2h0q

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(New page: 200px<br /><applet load="2h0q" size="350" color="white" frame="true" align="right" spinBox="true" caption="2h0q, resolution 1.82&Aring;" /> '''Crystal Structure of...)
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Revision as of 10:21, 23 January 2008

Image:2h0q.jpg

2h0q, resolution 1.82Å

Drag the structure with the mouse to rotate

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

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