Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 9417031.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
The function and regulation of the receptorlike transmembrane protein tyrosine phosphatases (RPTPs) are not well understood. Ligand-induced dimerization inhibited the function of the epidermal growth factor receptor (EGFR)-RPTP CD45 chimera (EGFR-CD45) in T cell signal transduction. Properties of mutated EGFR-CD45 chimeras supported a general model for the regulation of RPTPs, derived from the crystal structure of the RPTPalpha membrane-proximal phosphatase domain. The phosphatase domain apparently forms a symmetrical dimer in which the catalytic site of one molecule is blocked by specific contacts with a wedge from the other.
Medical subject headings
- Leukocyte Common Antigens
- Protein Tyrosine Phosphatases
- T-Lymphocytes