2IKQ
Crystal structure of mouse Sts-1 PGM domain in complex with phosphate
Summary for 2IKQ
| Entry DOI | 10.2210/pdb2ikq/pdb |
| Related | 2H0Q |
| Descriptor | Suppressor of T-cell receptor signaling 1, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | pgm; acid phosphatase; phospho-histidine enzyme, signaling protein, immune system |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm (By similarity): Q8BGG7 |
| Total number of polymer chains | 3 |
| Total formula weight | 91376.23 |
| Authors | Chen, Y.,Nassar, N. (deposition date: 2006-10-02, release date: 2007-08-14, Last modification date: 2023-08-30) |
| 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 Cited by 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: 17679096DOI: 10.1016/j.molcel.2007.06.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.609 Å) |
Structure validation
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