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.
|Authors||Church, W. B.;Lei, P. W.;Ogg, D. J.;Scott, K. F. :|
|Publisher Name||Acta Crystallogr D Biol Crystallogr|
|Published Issue||Pt 11|
|URL link to publisher's version||http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11053860|
|OpenAccess link to author's accepted manuscript version||https://publications.gimr.garvan.org.au/open-access/1331|