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

Stec B, Cheltsov A, Millán JL
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 866-70 (2010)
Related entries: 1zeb, 1zed, 1zef, 3mk1, 3mk2

Cited: 13 times
EuropePMC logo PMID: 20693656

Abstract

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. Biol. 350, 441-451] were re-refined. Significant variations in ligand positioning and identity were found compared with the previous report. 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. These improvements led to a change in the position of L-Phe at the peripheral binding site, which appeared to be reversed. 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. Comparison of the re-refined models shows a consistent pattern of interactions at the peripheral site.

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Related citations provided by authors (1)

  1. Structural studies of human placental alkaline phosphatase in complex with functional ligands.. Llinas P, Stura EA, Ménez A, Kiss Z, Stigbrand T, Millán JL, Le Du MH J Mol Biol 350 441-51 (2005)

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