PRODUCTION, CRYSTALLIZATION, AND PRELIMINARY-X-RAY ANALYSIS OF THE HUMAN MHC CLASS IB MOLECULE HLA-E

Citation
Ca. Ocallaghan et al., PRODUCTION, CRYSTALLIZATION, AND PRELIMINARY-X-RAY ANALYSIS OF THE HUMAN MHC CLASS IB MOLECULE HLA-E, Protein science, 7(5), 1998, pp. 1264-1266
Citations number
14
Categorie Soggetti
Biology
Journal title
ISSN journal
09618368
Volume
7
Issue
5
Year of publication
1998
Pages
1264 - 1266
Database
ISI
SICI code
0961-8368(1998)7:5<1264:PCAPAO>2.0.ZU;2-R
Abstract
HLA-E is the first human class Ib major histocompatibility complex mol ecule to be crystallized. HLA-E is highly conserved and almost nonpoly morphic, and has recently been shown to be the first specialized ligan d for natural killer cell receptors. In functional studies, HLA-E is u nlike the class Ia MHC molecules in having tightly restricted peptide binding specificity. HLA-E binds a limited set of almost identical lea der sequence peptides derived from class Ia molecules and presents the se at the cell surface for recognition by natural killer cell receptor s. We now show that the extracellular region of HLA-E forms a stable c omplex with beta 2 microglobulin and can be refolded around synthetic peptide. Crystals of this complex formed slowly over four to six month s in the presence of ammonium sulphate. The crystals diffract to 2.85 A with space group P3(1)21 and unit cell dimensions a = 182.2 Angstrom , b = 182.2 Angstrom, c = 88.4 Angstrom.