Crystallization and preliminary X-ray crystallographic analysis of human plasma platelet activating factor acetylhydrolase.
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.
Samanta
Uttamkumar
U
Department of Chemistry & Biochemistry, University of Delaware, Newark, DE 19716, USA.
Wilder
Cheryl
C
Bahnson
Brian J
BJ
D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans
D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase