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• W1668831292 abstract "Abstract Human recombinant interleukin-2 (IL-2) and a soluble recombinant form of the human p55 (Tac antigen) component of the IL-2 receptor (IL-2R) have been cocrystallized in 1.7-1.8 M ammonium sulfate, in the pH range 7.0-8.2. Variously glycosylated forms of both receptor and ligand can be cocrystallized under those conditions. The best crystals of the putative receptor-ligand complex involve the enzymatically desialylated receptor and unglycosylated IL-2. These crystals belong to the trigonal space group P3(1)2(1) or its enantiomorph, with unit cell dimensions a = b = 91 A and c = 119 A, and diffract to 3.5 A resolution. There is one receptor-ligand complex asymmetric unit, with a Matthews coefficient of 2.7, assuming the presence of one IL-2 molecule-receptor molecule. Interestingly, in addition to IL-2 (Mr = 14,000), the p55 IL-2 receptor (Mr = 44,000) and two fragments of the receptor, of apparent Mr = 35,000 and 25,000, respectively, in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the crystals are enriched in a reducible dimeric form of the desialylated receptor (apparent Mr = 90,000), as compared with protein solution from which the crystals grow. The overall amino acid content in the crystals is consistent with a 1:1 ratio of receptor to ligand. A native data set has been collected on a multiwire area detector and the search for suitable heavy atom derivatives is in progress." @default.
• W1668831292 created "2016-06-24" @default.
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• W1668831292 date "1989-07-01" @default.
• W1668831292 modified "2023-10-18" @default.
• W1668831292 title "Crystallization and Preliminary X-ray Diffraction Studies of a Complex between Interleukin-2 and a Soluble Form of the p55 Component of the High Affinity Interleukin-2 Receptor" @default.
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• W1668831292 doi "https://doi.org/10.1016/s0021-9258(18)63916-x" @default.
• W1668831292 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2787321" @default.
• W1668831292 hasPublicationYear "1989" @default.
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