title: Crystallization and preliminary X-ray diffraction studies of a new crystal form of human secretory type IIA phospholipase A2.
abstract: Human synovial type IIA phospholipase A(2) (sPLA(2)-IIA) has been implicated in the pathogenesis of a number of inflammatory diseases and is a target for the development of therapeutically useful inhibitors. Biochemical evidence suggests a novel mechanism of inhibition for a series of peptide inhibitors originally derived from the primary sequence of the protein. On co-incubation with one of these inhibitors, single crystals of a hitherto unreported crystallographic form of sPLA2-IIA suitable for diffraction analysis were obtained. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 140.8, b = 38.9, c = 109.1 A, beta = 125.1 degrees, and diffraction at 2.4 A resolution has been observed.
authors.affiliation: Arthritis and Inflammation Research Program, The Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, NSW 2010, Australia. b.church@garvan.unsw.edu.au
authors.forename: W B
authors.initials: WB
authors.lastname: Church
authors.forename: P W
authors.initials: PW
authors.lastname: Lei
authors.forename: D J
authors.initials: DJ
authors.lastname: Ogg
authors.forename: K F
authors.initials: KF
authors.lastname: Scott
mesh_terms: D003460:Crystallization; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D010741:Phospholipases A / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D054467:Phospholipases A2; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D004791:Enzyme Inhibitors; D010741:Phospholipases A; D054467:Phospholipases A2