Publications
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.
| 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 | http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11053860 |