2H0Q: Crystal Structure Of The Pgm Domain Of The Suppressor Of T-Cell Receptor (Sts-1)

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.
PDB ID: 2H0QDownload
MMDB ID: 60457
PDB Deposition Date: 2006/5/15
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.82  Å
Source Organism:
Similar Structures:
Biological Unit for 2H0Q: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2H0Q
Label Count Molecule
Proteins (2 molecules)
Suppressor of T-cell Receptor Signaling 1(Gene symbol: Ubash3b)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB