Sandbox89220: Difference between revisions

PMM2 converts mannose-6-phosphate into mannose-1-phosphate that would then serve as the building bloc of the dolichol-linked oligosaccharides for glycosylation in endoplasmic reticulum. It's not clear how PMM2 the cap and core domains would coordinate with each other. However,through the extrapolation of its paralogous protein, PMM1 which has a complex mechanism that uses charges of the conserved residues in the cap domains to sweep the substrate into core domain, we could postulate that PMM2 would utilize similar machinery<ref>Freeze,TOWARDS A THERAPY FOR PHOSPHOMANNOMUTASE 2 DEFECIENCY, THE DEFECT IN CDG-Ia PATIENTS [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2783247/?tool=pubmed]</ref>. Also, with the close resemblance to the PGM proteins, PMM2 might have similar machinery that manipulate the conformational changes that “closes” cap domain after binding substrates to allow the specificity loops getting into contact with the active site of the core domain, thus participating in catalysis.