2irt

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spinqualitylabelsall models 2irt, resolution 3.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

INITIAL CRYSTALLOGRAPHIC ANALYSES OF A RECOMBINANT INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

We report the crystallization of samples of a recombinant preparation of, human interleukin-1 receptor antagonist protein (IRAP) and solution of the, crystal structure by isomorphous replacement methods. Crystals were, obtained by the hanging-drop vapor-diffusion method at 277 K from, solutions of PEG 4000 containing sodium chloride, dithiothreitol and PIPES, [sodium piperazione-N,N'-bis(2-ethanesulfonate)] buffer at pH 7.0., Crystals appear within about a week and grow as truncated tetragonal, bipyramids to 0.3-0.6 mm on an edge. X-ray diffraction data from these, crystals specify space group P4(3)2(1)2 and unit-cell dimensions of a = b, = 72.35(26), c = 114.7(8) A and Z = 16 (two molecules per asymmetric, unit). Fresh crystals diffract to about 2.3 A resolution. The search for, heavy-atom derivatives has produced two, potassium gold cyanide and, trimethyl lead chloride, as same-site, single-site derivatives. Inspection, of an electron-density map at 4 A resolution calculated with these, derivatives confirms that the IRAP molecule is a member of the, interleukin-1 structural family.

Disease

Known diseases associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147679], Mental retardation, X-linked, 21/34 OMIM:[300206]

About this Structure

2IRT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Initial crystallographic analysis of a recombinant human interleukin-1 receptor antagonist protein., Clancy LL, Finzel BC, Yem AW, Deibel MR Jr, Strakalaitis NA, Brunner DP, Sweet RM, Einspahr HM, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):197-201. PMID:15299459

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