2IRT

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

Summary for 2IRT

• Entry DOI: 10.2210/pdb2irt/pdb
• Descriptor: INTERLEUKIN-1 RECEPTOR ANTAGONIST (1 entity in total)
• Functional Keywords: signal protein
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Secreted. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: P18510
• Total number of polymer chains: 2
• Total formula weight: 34290.81

Authors

Finzel, B.C.,Clancy, L.L.,Einspahr, H.M. (deposition date: 1994-07-13, release date: 1994-10-15, Last modification date: 2024-02-21)

Primary citation

Clancy, L.L.,Finzel, B.C.,Yem, A.W.,Deibel, M.R.,Strakalaitis, N.A.,Brunner, D.P.,Sweet, R.M.,Einspahr, H.M.
Initial crystallographic analysis of a recombinant human interleukin-1 receptor antagonist protein.
Acta Crystallogr.,Sect.D, 50:197-201, 1994

PubMed Abstract: 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.

PubMed: 15299459
DOI: 10.1107/S0907444993009394

Experimental method

X-RAY DIFFRACTION (3.2 Å)