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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 16, Issue 1, 2009

Page: [97 - 100] Pages: 4

DOI: 10.2174/092986609787049321

Price: $65

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.

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


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