Objetivo
The phosphorylation of tyrosine residues is an essential element of many signal transduction pathways triggered by hormones, mitogens, and oncogenes that lead to processes such as cell growth, proliferation, and differentiation. Protein phosphorylation is reversible and controlled by the opposing action of protein kinases and phosphatases that catalyze phosphorylation and dephosphorylation, respectively. In our work, we will investigate the crystal structure of a representative member of the receptor-like protein tyrosine phosphatase, namely, human PTPu, using X-ray diffraction techniques. This is particular interisting in light of the observation that the extracellular portion of PTPu, which is reminiscent of the extracellular portion of neural cell adhesion molecules (N-CAMs), participates in forming homophilic binding interactions. It is possible that signals resulting from cell-cell contacts may be transduced across the plasma membrane resulting in modulation of the catalytic activity of PTPu. It is of interest to understand the structure of PTPu which would provide insight into the structural mechanism of transmembrane signal transduction.
Ámbito científico
CORDIS clasifica los proyectos con EuroSciVoc, una taxonomía plurilingüe de ámbitos científicos, mediante un proceso semiautomático basado en técnicas de procesamiento del lenguaje natural.
CORDIS clasifica los proyectos con EuroSciVoc, una taxonomía plurilingüe de ámbitos científicos, mediante un proceso semiautomático basado en técnicas de procesamiento del lenguaje natural.
Convocatoria de propuestas
Data not availableRégimen de financiación
RGI - Research grants (individual fellowships)Coordinador
OX1 3QU Oxford
Reino Unido