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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.

Type Journal
ISBN 0907-4449 (Print)
Authors Church, W. B.;Lei, P. W.;Ogg, D. J.;Scott, K. F. :
Publisher Name Acta Crystallogr D Biol Crystallogr
Published Date 2000-01-01
Published Volume 56
Published Issue Pt 11
Published Pages 1482-4
Status Published in-print
URL link to publisher's version