Crystal structure of human recombinant interleukin-4 at 2.25 Å resolution

The crystal structure of human recombinant interleukin-4 (IL-4) has been solved by multiple isomorphous replacement, and refined to an R factor of 0.218 at 2.25 Å resolution. The molecule is a left-handed four-helix bundle with a short stretch of β sheet. The structure bears close resemblance to oth...

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Veröffentlicht in:	FEBS letters 1992-08, Vol.309 (1), p.59-64
Hauptverfasser:	Wlodaver, Alexander, Pavlovsky, Alexander, Gustchina, Alla
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analysis of the immune response. Humoral and cellular immunity Biological and medical sciences Cytokine Fundamental and applied biological sciences. Psychology Fundamental immunology Granulocyte-Macrophage Colony-Stimulating Factor - chemistry Humans Immunobiology Interleukin-4 - chemistry Lymphokines, interleukins ( function, expression) Protein Conformation Protein structure Recombinant Proteins - chemistry Refinement Regulatory factors and their cellular receptors Software X-ray crystallography X-Ray Diffraction - methods
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