PMID: 20693656

 

    Legend: Sugar

Title : Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site

Abstract :
  1. In order to gain deeper insights into the functional sites of human placental alkaline phosphatase , the structures of the enzyme with the putative regulators L- Phe , pNPP and 5'-AMP [Llinas et al. (2005), J. Mol
  2. Biol
  3. 350, 441-451] were re-refined
  4. Significant variations in ligand position ing and identity were found compared with the previous report
  5. The multiple corrections to the model improved the phases and the electron-density maps, allowing the modeling of omitted side chains and multiple disordered residues
  6. These improvements led to a change in the position of L- Phe at the peripheral binding site , which appeared to be reversed
  7. The structure with pNPP contained only p-nitrophenol in three distinct sites , while the structure with 5'-AMP contained the p-nitrophenyl group in two of the sites instead of 5'-AMP
  8. Comparison of the re-refined models shows a consistent pattern of interactions at the peripheral site