2H0Q

Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1)

Summary for 2H0Q

• Entry DOI: 10.2210/pdb2h0q/pdb
• Descriptor: Suppressor of T-cell receptor signaling 1 (2 entities in total)
• Functional Keywords: pgm, sts-1, signaling protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm (By similarity): Q8BGG7
• Total number of polymer chains: 3
• Total formula weight: 88102.94

Authors

Nassar, N.,Ford, B.,Carpino, N. (deposition date: 2006-05-15, release date: 2007-11-06, Last modification date: 2024-02-14)

Primary citation

Mikhailik, A.,Ford, B.,Keller, J.,Chen, Y.,Nassar, N.,Carpino, N.
A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling.
Mol.Cell, 27:486-497, 2007

PubMed Abstract: 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.

PubMed: 17679096
DOI: 10.1016/j.molcel.2007.06.015

Experimental method

X-RAY DIFFRACTION (1.82 Å)