Crystallization and preliminary X-ray diffraction studies of a new crystal form of human secretory type IIA phospholipase A2.
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.
Church
W B
WB
Arthritis and Inflammation Research Program, The Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, NSW 2010, Australia. b.church@garvan.unsw.edu.au
Lei
P W
PW
Ogg
D J
DJ
Scott
K F
KF
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
D004791:Enzyme Inhibitors; D010741:Phospholipases A; D054467:Phospholipases A2