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