Crystallization and preliminary X-ray crystallographic analysis of human plasma platelet activating factor acetylhydrolase

Protein Pept Lett. 2009;16(1):97-100. doi: 10.2174/092986609787049321.

Abstract

The plasma form of the human enzyme platelet activating factor acetylhydrolase (PAF-AH) has been crystallized, and X-ray diffraction data were collected at a synchrotron source to a resolution of 1.47 A. The crystals belong to space group C2, with unit cell parameters of a = 116.18, b = 83.06, c = 96.71 A, and beta= 115.09 degrees and two molecules in the asymmetric unit. PAF-AH functions as a general anti-inflammatory scavenger by reducing the levels of the signaling molecule PAF. Additionally, the LDL bound enzyme has been linked to atherosclerosis due to its hydrolytic activities of pro-inflammatory agents, such as sn-2 oxidatively fragmented phospholipids.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • 1-Alkyl-2-acetylglycerophosphocholine Esterase / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Humans

Substances

  • 1-Alkyl-2-acetylglycerophosphocholine Esterase