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Protein Science, Vol 7, Issue 4 1057-1060, Copyright © 1998 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary X-ray analysis of a 1:1 complex between a designed monomeric interferon-gamma and its soluble receptor

M. RANDAL and A. A. KOSSIAKOFF
Graduate Group in Biophysics, University of California, San Francisco, California 94000

A variant of human interferon-gamma (IFN-{gamma}) has been created in which the two chains of the homodimeric cytokine were linked N-to C-terminus by an eight residue polypeptide linker. The sequence of this linker was derived from a loop in bira bifunctional protein, and was determined from a structural database search. This ``single-chain'' variant was used to create an IFN-{gamma} molecule that binds only a single copy of the {alpha}-chain receptor, rather than the 2 {alpha}-chain receptor: 1 IFN-{gamma} binding stoichiometry observed for the native hormone. Crystals have been grown of a 1:1 complex between this single-chain molecule and the extracellular domain of its {alpha}-chain receptor. These crystals diffract beyond 2.0 A, significantly better than the 2.9 A observed for the native 2:1 complex. Density calculations suggest these crystals contain two complexes in the asymmetric unit; a self-rotation function confirms this conclusion.
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C. D. Krause, C. A. Lunn, L. S. Izotova, O. Mirochnitchenko, S. V. Kotenko, D. J. Lundell, S. K. Narula, and S. Pestka
Signaling by Covalent Heterodimers of Interferon-gamma . EVIDENCE FOR ONE-SIDED SIGNALING IN THE ACTIVE TETRAMERIC RECEPTOR COMPLEX
J. Biol. Chem., July 21, 2000; 275(30): 22995 - 23004.
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