Crystallization and Preliminary X-Ray Crystallographic Analysis of Human Plasma Platelet Activating Factor Acetylhydrolase

Title: Crystallization and Preliminary X-Ray Crystallographic Analysis of Human Plasma Platelet Activating Factor Acetylhydrolase

Volume: 16 Issue: 1

Author(s): Uttamkumar Samanta, Cheryl Wilder and Brian J. Bahnson

Affiliation:

Keywords: PAF-AH, lipoprotein associated phospholipase A2, Lp-PLA2, group VIIA PLA2, crystallization

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 Å. The crystals belong to space group C2, with unit cell parameters of a = 116.18, b = 83.06, c = 96.71 Å, and β = 115.09° 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.

Cite this article as:

Samanta Uttamkumar, Wilder Cheryl and Bahnson J. Brian, Crystallization and Preliminary X-Ray Crystallographic Analysis of Human Plasma Platelet Activating Factor Acetylhydrolase, Protein & Peptide Letters 2009; 16 (1) . https://dx.doi.org/10.2174/092986609787049321